Crystal Structure of the Pro Form of a Matrix Metalloproteinase and an Allosteric Processing Inhibitor

ABSTRACT

The present invention includes a crystal comprising a complex of the pro form of a matrix metalloprotease (proMMP) and a small-molecule allosteric processing inhibitor that inhibits that activation of the proMMP, methods for identifying small-molecule allosteric processing inhibitors that inhibit the activation of a proMMP, and methods of treatment using small-molecule allosteric processing inhibitors that inhibit the activation of a proMMP. The present invention relates to the crystal structure of a complex of proMMP9 bound to a small-molecule allosteric processing inhibitor that inhibits activation of proMMP9. The invention further relates to the use of the methods and the crystal and related structural information for designing, selecting and/or optimizing small-molecule allosteric processing inhibitors that inhibit activation of proMMP9 and proMMP9 homologues. The present invention also relates to the use of small-molecule allosteric processing inhibitors for the treatment of diseases mediated by inappropriate matrix metalloproteinase (MMP) activity.

CROSS REFERENCE TO RELATED APPLICATION

This application claims priority to provisional application Ser. No. 61/502,516, filed Jun. 29, 2011, which is incorporated herein by reference in its entirety.

TECHNICAL FIELD

The present invention generally pertains to the fields of high-throughput screening, protein crystallization, X-ray diffraction analysis, three-dimensional structure determination, molecular modeling, and structure based rational drug design. More particularly, the present invention pertains to methods for selecting ligands that are allosteric processing inhibitors that inhibit activation of the pro form of matrix metalloproteinases (proMMPs) and to the therapeutic and prophylactic uses of the selected ligands. Examples of relevant therapeutic areas generally include inflammation, oncology, cardiovascular disease, and neurological disorders.

BACKGROUND OF THE INVENTION

Various publications, which may include patents, published applications, technical articles and scholarly articles, are cited throughout the specification in parentheses, and full citations of each may be found at the end of the specification. Each of these cited publications is incorporated by reference herein, in its entirety.

Matrix metalloproteinases (MMPs) are a family of structurally related zinc-dependent proteolytic enzymes that digest extracellular matrix proteins such as collagen, elastin, laminin and fibronectin. Currently, at least 28 different mammalian MMP proteins have been identified and they are grouped based on substrate specificity and domain structure. Enzymatic activities of the MMPs are precisely controlled, not only by their gene expression in various cell types, but also by activation of their inactive zymogen precursors (proMMPs) and inhibition by endogenous inhibitors and tissue inhibitors of metalloproteinases (TIMPs). The enzymes play a key role in normal homeostatic tissue remodeling events, but are also considered to play a key role in pathological destruction of the matrix in many connective tissue diseases such as arthritis, periodontitis, and tissue ulceration and also in cancer cell invasion and metastasis.

A role for MMPs in oncology is well established, as up-regulation of any number of MMPs are one mechanism by which malignant cells can overcome connective tissue barriers and metastasize (Vihinen, Ala-aho et al. 2005). MMPs also appear to have a direct role in angiogenesis, which is another reason they have been an important target for oncology indications (Handsley and Edwards 2005; Rundhaug 2005). Several different classes of MMPs are involved in these processes, including for example MMP9, MMP2, and MT1-MMP.

Other MMP mediated indications include the cartilage and bone degeneration that results in osteoarthritis and rheumatoid arthritis. The degeneration is due primarily to MMP digestion of the extracellular matrix (ECM) in bone and joints (Iannone and Lapadula 2003). MMP1, MMP3, MMP9, and MMP13 have all been found to be elevated in the tissues and body fluids surrounding the damaged areas.

MMPs may also have a role in cardiovascular diseases, in that they are believed to be involved in atherosclerotic plaque rupture, aneurysm and vascular and myocardial tissue morphogenesis (George 2000; Tayebjee, Lip et al. 2005). Elevated levels of MMP1, MMP2, MMP9, and MMP13 have often been associated with these conditions. Several other pathologies such as gastric ulcers, pulmonary hypertension, chronic obstructive pulmonary disease, inflammatory bowel disease, periodontal disease, skin ulcers, liver fibrosis, emphysema, and Marfan syndrome all appear to have an MMP component as well (Shah, Wilkin et al. 2002).

Within the central nervous system, altered MMP expression has been linked to several neurodegenerative disease states (Yong 1999), most notably in stroke (Cunningham, Wetzel et al. 2005). In particular, MMP2 and MMP9 appear to have the significant impact in propagating the brain tissue damage that occurs following an ischemic or hemorrhagic insult. Studies in human stroke patients and in animal stroke models have demonstrated that both MMP2 and MMP9 expression levels and activity increase sharply over a 24 hour period following an ischemic event. Within the brain, the microvascular endothelial cell tight junctions are broken down by activated MMP2 and MMP9, which results in increased permeability of the blood-brain barrier (BBB). This breakdown in the integrity of the BBB then leads to edema and infiltration of inflammatory agents, both of which cause increased cell death around the infarct core (the penumbra) and increase the possibility of hemorrhagic transformation. Administration of MMP inhibitors has been shown to be protective in animal models of stroke (Yong 1999; Gu, Cui et al. 2005). In addition, MMP9 knockout animals also demonstrate significant neuroprotection in similar stroke models (Asahi, Asahi et al. 2000). In the US, stroke is the third leading cause of mortality, and the leading cause of disability. Thus this area has a large unmet medical need for acute interventional therapy that could potentially be addressed with MMP inhibitors.

It has also been suggested that MMP9 may play a role in the progression of multiple sclerosis (MS). Studies have indicated that serum levels of MMP9 are elevated in active patients, and are concentrated around MS lesions (Opdenakker, Nelissen et al. 2003). Increased serum MMP9 activity would promote infiltration of leukocytes into the CNS, a causal factor and one of the hallmarks of the disease. MMPs may also contribute to severity and prolongation of migraines. In animal models of migraine (cortical spreading depression), MMP9 is rapidly upregulated and activated leading to a breakdown in the BBB, which results in mild to moderate edema (Gursoy-Ozdemir, Qiu et al. 2004). It is this brain swelling and subsequent vasoconstriction which causes the debilitating headaches and other symptoms associated with migraine. In the cortical spreading depression model, MMP inhibitors have been shown to prevent the opening of the BBB (Gursoy-Ozdemir, Qiu et al. 2004). Related research has shown that MMP9 is specifically upregulated in damaged brain tissues following traumatic brain injury (Wang, Mori et al. 2002), which would be predicted to lead to further brain damage due to edema and immune cell infiltration. MMPs may also have additional roles in additional chronic CNS disorders. In an animal model of Parkinson's disease, MMP9 was found to be rapidly upregulated after striatal injection of a dopaminergic neuron poison (MPTP) (Lorenzl, Calingasan et al. 2004), and MMP3 has been shown to process α-synuclein to an aggregation-prone form (Sung, Park et al. 2005). This implicates MMPs in both the neuronal remodeling that occurs upon cell loss and one of the potential causative factors of the disease. In patients with Alzheimer's disease, MMP9 was found to be upregulated in postmortem plasma samples compared to normal controls (Yong 1999; Lorenzl, Albers et al. 2003). Furthermore, pathologic expression of amyloid beta peptides induces expression and activation of MMP2, which may contribute to cerebral amyloid angiopathy, a major pathological feature of Alzheimer's disease (Jung, Zhang et al. 2003). MMPs may also have a role in vascular dementia, as MMP9 levels have been found to be elevated in the cerebrospinal fluid from demented patients (Adair, Charlie et al. 2004).

With regard to structure and activation of the inactive zymogen form, a prototypical MMP is matrix metalloproteinase 9 (MMP9). MMP9 is also known as macrophage gelatinase, gelatinase B, 92 kDa gelatinase, 92 kDa type IV collagenase, and type V collagenase. The inactive form of MMP9, proMMP9, is expressed with several different domains including a signal sequence for secretion, a propeptide domain which inhibits activity of proMMP9, a catalytic domain for protein cleavage, a fibronectin type-II (FnII) domain consisting of three fibronectin-type II repeats, and a hemopexin-like domain thought to assist in substrate docking The hemopexin-like domain also serves as a binding domain for interaction with Tissue Inhibitors of Metaloproteinases (TIMPs). The inactive zymogen form of MMP9, proMMP9, is maintained through a cysteine-switch mechanism, in which a Cys in the propeptide forms a complex with the catalytic zinc in the catalytic domain and occludes the active site (Van Wart and Birkedal-Hansen 1990). Activation of proMMP9 occurs in a two-step process. A protease cleaves an initial site after Met 60, disrupting the zinc coordination and destabilizing the propeptide interaction with the catalytic domain. This initial cleavage allows access to the second cleavage site at Phe 107, after which the propeptide is removed and the mature active form of the enzyme is released (Nagase 1997). The identity of the MMP9 activating proteases is unknown in vivo, although there is evidence that activation can occur through the actions of MMP3, chymase and trypsin (Ogata, Enghild et al. 1992; Fang, Raymond et al. 1997; Tchougounova, Lundequist et al. 2005).

Crystal structures of MMP9 and proMMP9 have been reported. A structure of the C-terminally truncated proMMP9 was reported to 2.5 Å resolution (Elkins, Ho et al. 2002). The structure contained the pro domain, the catalytic domain and the fibronectin-type II (FnII) repeats, but the structure did not contain active site inhibitors or allosteric processing inhibitors. Two additional publications reported the structure of the catalytic domain of MMP9 without the FnII repeats (Rowsell, Hawtin et al. 2002; Tochowicz, Maskos et al. 2007). The structures of the MMP9 catalytic domain showed both the apo and active site inhibited forms of the protein. The structures solved to date show a high degree of structural homology. No large difference in structure was noted due to the presence or lack of the FnII repeats. No structure reported to date identifies compounds binding to the region near residue Phe 107. In addition to the proMMP9 structure, the structures of proMMP1 (Jozic, Bourenkov et al. 2005), proMMP2 (Morgunova, Tuuttila et al. 1999), and proMMP3 (Becker, Marcy et al. 1995) have also been reported.

Based on the demonstrated involvement in numerous pathological conditions, inhibitors of matrix metalloproteases (MMPs) have been widely sought for their therapeutic potential in a range of disease states. However, non-selective active site MMP inhibitors have performed poorly in clinical trials. The failures have often been caused by dose-limiting toxicity and the manifestation of significant side effects, including the development of musculoskeletal syndrome (MSS). It has been suggested that development of more selective MMP inhibitors might help to overcome some of the problems that hindered clinical success in the past, but there are a number of obstacles to developing more selective MMP active site inhibitors. MMPs share a catalytically important Zn2+ ion in the active site and a highly conserved zinc-binding motif. In addition, there is considerable sequence conservation across the entire catalytic domain for members of the MMP family.

Herein is described a novel approach to developing more selective MMP inhibitors by targeting the pro domain of the inactive zymogens, proMMPs, with small-molecule allosteric processing inhibitors that bind and stabilize the inactive pro form of the protein and inhibit processing to the active enzyme. There is significantly less sequence identity within the pro domains of MMP proteins, no catalytically important Zn2+ ion, and no highly conserved zinc-binding motif. Thus targeting the pro domain of proMMPs is an attractive mechanism of action for inhibiting the activity of the MMP proteins Inhibition of proMMP9 activation has been observed with a specific monoclonal antibody (Ramos-DeSimone, Moll et al. 1993). The activation of proMMP9 by trypsin has also been shown to be inhibited by Bowman-Birk inhibitor proteins and derived peptide inhibitors (Losso, Munene et al. 2004). There are no reports, however, of small-molecule allosteric processing inhibitors that inhibit the proteolytic activation of proMMP9 or any other proMMP. The present invention provides methods of identifying such small-molecule allosteric processing inhibitors and methods of treatment using such inhibitors.

SUMMARY OF THE INVENTION

In one embodiment, the present invention comprises a crystal comprising the pro form of a matrix metalloproteinase (proMMP), or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP.

In another embodiment, the present invention comprises a crystal comprising proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of proMMP9.

In another embodiment, the present invention comprises a crystal comprising proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by phenylalanine (Phe) 107 in the apo form of proMMP9, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises a crystal comprising proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises a crystal comprising a homologue of proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the homologue of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is homologous to the region of space occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a crystal comprising the proMMP9 or a fragment, or target structural motif or derivative thereof, and a small-molecule allosteric processing inhibitor of proMMP9, wherein said fragment or derivative thereof is a peptide comprising SEQ ID NO:12 or a peptide having at least 95% sequence identity to SEQ ID NO:12.

In another embodiment, the present invention comprises a crystal comprising a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said crystal has a spacegroup of C2.

In another embodiment, the present invention comprises a crystal comprising a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said chemical entity is selected from the group consisting of the following structures:

Example 1

Example 2

Example 3

Example 4

In another embodiment, the present invention comprises a crystal comprising a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said crystal comprises a unit cell having dimensions selected from the group consisting of: the unit cell dimensions of a=91.7 (Å), b=73.7 (Å), c=79.4 (Å), the unit cell dimensions of a=90.7 (Å), b=73.0 (Å), c=78.2 (Å), the unit cell dimensions of a=91.0 (Å), b=73.6 (Å), c=78.0 (Å), and the unit cell dimensions of a=90.0 (Å), b=77.1 (Å), c=75.0 (Å).

In another embodiment, the present invention comprises an atomic structure of a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said atomic structure comprises coordinates selected form the group consisting of: the coordinates of Table 11, the coordinates of Table 12, the coordinates of Table 13, and the coordinates of Table 14.

In another embodiment, the present invention comprises an atomic structure of a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said proMMP is proMMP9.

In another embodiment, the present invention comprises an atomic structure of proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises an atomic structure of proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises an atomic structure of a proMMP, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the proMMP, and wherein said proMMP is a homologue of proMMP9 selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13.

In another embodiment, the present invention comprises an atomic structure of a homologue of proMMP9, or a fragment, or target structural motif or derivative thereof, and a chemical entity, wherein said chemical entity is a small-molecule allosteric processing inhibitor of the homologue of proMMP9, and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is homologous to the region of space occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of proMMP9 comprising the steps of: (a.) employing the structural coordinates of the allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding pocket on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying said allosteric binding site of proMMP9, wherein said allosteric binding site comprises a region of space that is occupied by phenylalanine (Phe) 107 in the apo form of proMMP9, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); (c.) employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.

In another embodiment, the present invention comprises a method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of proMMP9 comprising the steps of: (a.) employing the structural coordinates of the allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding pocket on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying said allosteric binding site of proMMP9, wherein said allosteric binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); (c.) employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.

In another embodiment, the present invention comprises a method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of a homologue of proMMP9 comprising the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of said homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying said allosteric binding site of the homologue of proMMP9, wherein said allosteric binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.

In another embodiment, the present invention comprises a method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of a homologue of proMMP9 comprising the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of said homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying said allosteric binding site of the homologue of proMMP9, wherein said allosteric binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); (c.) employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.

In another embodiment, the present invention comprises a method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of a homologue of proMMP9, wherein said homologue of proMMP9 is selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13, and wherein said method comprises the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of said homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying said allosteric binding site of the homologue of proMMP9, wherein said allosteric binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.

In another embodiment, the present invention comprises a method for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9 comprising the steps of: (a.) employing the structural coordinates of said allosteric binding site of proMMP9 according to any to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying a binding site for said chemical entity, wherein said binding site comprises a region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between the chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9 comprising the steps of: (a.) employing the structural coordinates of said allosteric binding site of proMMP9 according to any to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying a binding site for said chemical entity, wherein said binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between the chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9 comprising the steps of: (a.) employing the structural coordinates of proMMP9 according to any to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; (b.) identifying a binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between the chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: (a.) employing the structural coordinates of said allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: (a.) employing the structural coordinates of said allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site, (e) repeating steps (a) through (d) with a second chemical entity; and (f) selecting at least one part of said first or second chemical entity that associates with said all or part of said allosteric binding site based on said quantitated association of said first or second chemical entity.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site; (e) repeating steps (a) through (d) with a second chemical entity; and (f) selecting at least one part of said first or second chemical entity that associates with said all or part of said allosteric binding site based on said quantitated association of said first or second chemical entity.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9, wherein said homologue of MMP9 is selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13, and wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site.

In another embodiment, the present invention comprises a method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9, wherein said homologue of MMP9 is selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13, and wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, wherein said method comprises the steps of: (a.) employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on said computer; (b.) identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; (c.) employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); (d.) analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site; (e) repeating steps (a) through (d) with a second chemical entity; and (f) selecting at least one part of said first or second chemical entity that associates with said all or part of said allosteric binding site based on said quantitated association of said first or second chemical entity.

In another embodiment, the present invention comprises a method of inhibiting activation of a pro matrix metalloprotease (proMMP) using a chemical entity selected from the group consisting of: a small-molecule allosteric processing inhibitor and solvates, hydrates, tautomers, or pharmaceutically acceptable salts thereof.

In another embodiment, the present invention comprises a method of inhibiting activation of a proMMP using a pharmaceutical composition, comprising a small-molecule allosteric processing inhibitor and a pharmaceutically acceptable carrier.

In another embodiment, the present invention comprises a method of inhibiting activation of a proMMP using a chemical entity selected from the group consisting of: a small-molecule allosteric processing inhibitor and solvates, hydrates, tautomers, or pharmaceutically acceptable salts thereof; wherein said proMMP is proMMP9; and wherein said chemical entity binds in an allosteric binding site comprising a region of space that is occupied by phenylalanine (Phe) 107 in the apo form of proMMP9, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises a method of inhibiting activation of a proMMP using a chemical entity selected from the group consisting of: a small-molecule allosteric processing inhibitor and solvates, hydrates, tautomers, or pharmaceutically acceptable salts thereof; wherein said proMMP is proMMP9; and wherein said chemical entity binds in an allosteric binding site comprising amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises a method of inhibiting activation of a proMMP using a pharmaceutical composition, comprising a small-molecule allosteric processing inhibitor and a pharmaceutically acceptable carrier; wherein said proMMP is proMMP9; and wherein said chemical entity binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of inhibiting activation of a pro matrix metalloprotease (proMMP) using a chemical entity selected from the group consisting of: a small-molecule allosteric processing inhibitor and solvates, hydrates, tautomers, or pharmaceutically acceptable salts thereof; wherein said proMMP is a homologue of MMP9 selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13; and wherein said chemical entity binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of inhibiting activation of a proMMP using a pharmaceutical composition, comprising a small-molecule allosteric processing inhibitor and a pharmaceutically acceptable carrier; wherein said proMMP is a homologue of MMP9 selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13; and wherein said chemical entity binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of inhibiting matrix metalloprotease (MMP) activity in a mammal by administration of an effective amount of at least one small-molecule allosteric processing inhibitor that inhibits activation of the MMP.

In another embodiment, the present invention comprises a method of inhibiting matrix metalloprotease (MMP) activity in a mammal by administration of an effective amount of at least one small-molecule allosteric processing inhibitor that inhibits activation of the MMP; wherein said MMP is MMP9; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9

In another embodiment, the present invention comprises a method of inhibiting matrix metalloprotease (MMP) activity in a mammal by administration of an effective amount of at least one small-molecule allosteric processing inhibitor that inhibits activation of the MMP; wherein said MMP is MMP9; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).

In another embodiment, the present invention comprises a method of inhibiting matrix metalloprotease (MMP) activity in a mammal by administration of an effective amount of at least one small-molecule allosteric processing inhibitor that inhibits activation of the MMP; wherein said MMP is a homologue of MMP9 selected from the group consisting of: MMP1, MMP2, MMP3, and MMP13; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease wherein said syndrome, disorder or disease is associated with elevated MMP expression or MMP overexpression, or is a condition that accompanies syndromes, disorders or diseases associated with elevated MMP expression or MMP overexpression comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said syndrome, disorder or disease is selected from the group consisting of: neoplastic disorders, osteoarthritis, rheumatoid arthritis, cardiovascular diseases, gastric ulcer, pulmonary hypertension, chronic obstructive pulmonary disease, inflammatory bowel syndrome, periodontal disease, skin ulcers, liver fibrosis, emphysema, Marfan syndrome, stroke, multiple sclerosis, asthma, abdominal aortic aneurysm, coronary artery disease, idiopathic pulmonary fibrosis, renal fibrosis, and migraine, comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor.

In another embodiment, the present invention comprises a method of inhibiting matrix metalloprotease (MMP) activity in a mammal by administration of an effective amount of at least one small-molecule allosteric processing inhibitor that inhibits activation of the MMP; wherein said MMP is a homologue of MMP9 selected from the group consisting of: MMP1, MMP2, MMP3, and MMP13; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is MMP9; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease wherein said syndrome, disorder or disease is associated with elevated MMP expression or MMP overexpression, or is a condition that accompanies syndromes, disorders or diseases associated with elevated MMP expression or MMP overexpression comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is MMP9; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said syndrome, disorder or disease is selected from the group consisting of: neoplastic disorders, osteoarthritis, rheumatoid arthritis, cardiovascular diseases, gastric ulcer, pulmonary hypertension, chronic obstructive pulmonary disease, inflammatory bowel syndrome, periodontal disease, skin ulcers, liver fibrosis, emphysema, Marfan syndrome, stroke, multiple sclerosis, asthma, abdominal aortic aneurysm, coronary artery disease, idiopathic pulmonary fibrosis, renal fibrosis, and migraine, comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is MMP9; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is a homologue of MMP9 selected from the group consisting of: MMP1, MMP2, MMP3, and MMP13; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method for preventing, treating or ameliorating an MMP mediated syndrome, disorder or disease wherein said syndrome, disorder or disease is associated with elevated MMP expression or MMP overexpression, or is a condition that accompanies syndromes, disorders or diseases associated with elevated MMP expression or MMP overexpression comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of the MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is a homologue of MMP9 selected from the group consisting of: MMP1, MMP2, MMP3, and MMP13; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said syndrome, disorder or disease is selected from the group consisting of: neoplastic disorders, osteoarthritis, rheumatoid arthritis, cardiovascular diseases, gastric ulcer, pulmonary hypertension, chronic obstructive pulmonary disease, inflammatory bowel syndrome, periodontal disease, skin ulcers, liver fibrosis, emphysema, Marfan syndrome, stroke, multiple sclerosis, asthma, abdominal aortic aneurysm, coronary artery disease, idiopathic pulmonary fibrosis, renal fibrosis, and migraine, comprising administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said MMP is a homologue of MMP9 selected from the group consisting of: MMP1, MMP2, MMP3, and MMP13; and wherein said small-molecule allosteric processing inhibitor binds in an allosteric binding site comprising a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said syndrome, disorder or disease is a neoplastic disorder, which is ovarian cancer.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; wherein said syndrome, disorder or disease is a cardiovascular disease, and wherein said cardiovascular disease is selected from the group consisting of: atherosclerotic plaque rupture, aneurysm, vascular tissue morphogenesis, coronary artery disease, and myocardial tissue morphogenesis.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is a cardiovascular disease, and wherein said cardiovascular disease is atherosclerotic plaque rupture.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is rheumatoid arthritis.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is asthma.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is chronic obstructive pulmonary disease.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is inflammatory bowel syndrome.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is abdominal aortic aneurism.

In another embodiment, the present invention comprises a method of preventing, treating or ameliorating a syndrome, disorder or disease, wherein said method comprises administering to a subject in need thereof an effective amount of a small-molecule allosteric processing inhibitor that inhibits activation of an MMP, or a form, composition or medicament comprising the allosteric processing inhibitor; and wherein said syndrome, disorder or disease is osteoarthritis.

Additional embodiments and advantages of the invention will become apparent from the detailed discussion, schemes, examples, and claims included herein.

BRIEF DESCRIPTION OF THE DRAWINGS

Embodiments of the present invention will now be described, by way of an example only, with reference to the accompanying drawings wherein:

FIG. 1: Shown are western blots with two different antibodies illustrating the effects of a small-molecule allosteric processing inhibitor, Example 2, on the activation of proMMP9 in synoviocytes harvested from female Lewis rats after inducing arthritis with i.p. administration of Streptococcal cell wall peptidoglycan polysaccharides. A mouse monoclonal antibody, mAb L51/82, detected pro and processed forms of MMP9. The mouse monoclonal antibody showed that Example 2 caused a dose-dependent reduction in the appearance of the 80 kD active form of MMP9 and the appearance of an 86 kD form of the protein (FIG. 1A, lanes 3-6). A rabbit polyclonal antibody, pAb-1246, detected the 80 kD active form of MMP9, but did not recognize the 100 kD form of proMMP9. The rabbit polyclonal antibody showed that the small-molecule allosteric processing inhibitor caused a dose-dependent reduction in the appearance of the 80 kD active form of MMP9 (FIG. 1B, lanes 2-6).

FIG. 2: Shown are western blots illustrating increased proMMP9 and increased active MMP9 in tibia-tarsus joints (ankles) from female Lewis rats after inducing arthritis with i.p. administration of Streptococcal cell wall peptidoglycan polysaccharides (SCW). In healthy ankles of rats administered saline, mAb-L51/82 detected small amounts of an approximately 100 kD proMMP9 and an approximately 80 kD form of active MMP9 (FIG. 2A, lanes 1 and 2). The amount of proMMP9 increased markedly in ankle homogenates 5 and 18 days after SCW-administration (FIG. 2A, lanes 3-5 and 6-8, respectively). The amount of active 80 kD MMP9 increased mildly 5 days after SCW-administration (FIG. 2A, lanes 3-5) and increased markedly 18 days after SCW-administration (FIG. 2A, lanes 6-8). In healthy ankles of rats administered saline, mAb-1246 detected small amounts active 80 kD MMP9 (FIG. 2B, lanes 1 and 2). The 80 kD active MMP9 increased mildly 5 days after SCW-administration (FIG. 2A, lanes 3-5) and increased markedly 18 days after SCW-administration (FIG. 2A, lanes 6-8).

FIG. 3: Shown are western blots with two different antibodies illustrating the effects of a small-molecule allosteric processing inhibitor, Example 2, on the activation of proMMP9 in tibia-tarsus joints (ankles) from female Lewis rats after inducing arthritis with i.p. administration of Streptococcal cell wall peptidoglycan polysaccharides (SCW). Both proMMP9 and active MMP9 were abundantly present in ankles of SCW-induced vehicle-treated rats (FIGS. 3A and 3B, lanes 1-3). Treatment of rats with Example 2 did not reduce the abundance of proMMP-9 (FIG. 3A, lanes 4-9). However, treatment of rats with Example 2 resulted in a notable reduction in the active 80 kD form of MMP9 detected with pAb-1246 (FIG. 3B, lanes 4-9) and also with mAb-L51/82 (FIG. 3A, lanes 4-9).

FIGS. 4 (A, B, and C): Shown are three separate superpositions of inhibited proMMP9 (dark structure) with apo proMMP9 (light structure). While the exact location of the displaced loop can vary with the different inhibitors, all of the inhibitors bind in the same pocket and prevent the cleavage of the bond to form an active enzyme. A is the proMMP9 complex with Example 2, B is the proMMP9 complex with Example 3, and C is the proMMP9 complex with Example 4.

FIG. 5: Shown are the superpositions of the structures for inhibited proMMP9 with apo proMMP9 (marked structure). The structures are shown as ribbon cartoons with the inhibitors shown as ball and stick figures. While the exact location of the displaced loop can vary with the different inhibitors, all of the inhibitors bind in the same pocket and prevent the cleavage of the bond to form an active enzyme. The inhibitors shown are Example 2, Example 3, and Example 4.

FIG. 6: Shown is the accessible surface of the proMMP9 structure. The surface of contact for the residues in the catalytic domain are colored a dark gray and the contact surface from the residues of the pro domain are colored a medium gray.

FIG. 7: Shown is the structural overlap of the proMMP structures that have been determined. The overlap demonstrates that a similar tertiary structure exists for other MMP pro domains with the final cleavage site for activation in contact with the catalytic domain.

FIG. 8: Shown is the sequence alignment of the pro domains for the human MMP family. The tertiary structure for these domains is a four helical bundle in the determined structures and predicted to have the same fold from the sequence for the remaining MMPs. While there are a variety of residues that fill the cavity in the catalytic domain the general mode of stabilization will remain the same.

DEFINITIONS

As is generally the case in biotechnology and chemistry, the description of the present invention has required the use of a number of terms of art. Although it is not practical to do so exhaustively, definitions for some of these terms are provided here for ease of reference. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Definitions for other terms may also appear elsewhere herein. However, the definitions provided here and elsewhere herein should always be considered in determining the intended scope and meaning of the defined terms. Although any methods and materials similar or equivalent to those described herein can be used in the practice of the present invention, the preferred methods and materials are described.

The term “comprising” means “including principally, but not necessarily solely”. Furthermore, variations of the word “comprising”, such as “comprise” and “comprises”, have correspondingly varied meanings.

As used herein, the terms “containing”, “having” and “including” are used in their open, non-limiting sense.

As used herein, “sequence” means the linear order in which monomers occur in a polymer, for example, the order of amino acids in a polypeptide or the order of nucleotides in a polynucleotide.

The terms “polypeptide”, “protein”, and “peptide” are used herein interchangeably to refer to amino acid chains in which the amino acid residues are linked by peptide bonds or modified peptide bonds. The amino acid chains can be of any length of greater than two amino acids. Unless otherwise specified, the terms “polypeptide”, “protein”, and “peptide” also encompass various modified forms thereof. Such modified forms may be naturally occurring modified forms or chemically modified forms. Examples of modified forms include, but are not limited to, glycosylated forms, phosphorylated forms, myristoylated forms, palmitoylated forms, ribosylated forms, acetylated forms, ubiquitinated forms, etc. Modifications also include intra-molecular crosslinking and covalent attachment to various moieties such as lipids, flavin, biotin, polyethylene glycol or derivatives thereof, etc. In addition, modifications may also include cyclization, branching and cross-linking Further, amino acids other than the conventional twenty amino acids encoded by the codons of genes may also be included in a polypeptide.

As used herein, a protein or nucleic acid molecule is said to be “isolated” when the protein or nucleic acid molecule is substantially separated from contaminants from the source of the protein or nucleic acid.

As used herein, the term “native protein” refers to a protein comprising an amino acid sequence identical to that of a protein isolated from its natural source or organism.

As used herein, the term “amino acids” refers to the L-isomers of the naturally occurring amino acids. The naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, γ-carboxyglutamic acid, arginine, ornithine, and lysine. Unless specifically indicated, all amino acids are referred to in this application are in the L-form.

As used herein, the term “normatural amino acids” refers to amino acids that are not naturally found in proteins. For example, selenomethionine.

As used herein, the term “positively charged amino acid” includes any amino acids having a positively charged side chain under normal physiological conditions. Examples of positively charged naturally occurring amino acids are arginine, lysine, and histidine.

As used herein, the term “negatively charged amino acid” includes any amino acids having a negatively charged side chains under normal physiological conditions. Examples of negatively charged naturally occurring amino acids are aspartic acid and glutamic acid.

As used herein, the term “hydrophobic amino acid” includes any amino acids having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine.

As used herein, the term “hydrophilic amino acid” refers to any amino acids having an uncharged, polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids are serine, threonine, tyrosine, asparagine, glutamine and cysteine.

As used herein, “nucleic acid” is defined as RNA or DNA that encodes a protein or peptide as defined herein, or is complementary to nucleic acid sequence encoding such peptides, or hybridizes to such nucleic acid and remains stably bound to it under appropriate stringency conditions. Nucleic acid sequences can be composed of natural nucleotides of the following bases: thymidine, adenine, cytosine, guanine, and uracil; abbreviated T, A, C, G, and U, respectively, and/or synthetic analogs of the natural nucleotides.

The term “oligonucleotide” or “oligo” refers to a single-stranded DNA or RNA sequence of a relatively short length, for example, less than 100 residues long. For many methods, oligonucleotides of about 16-25 nucleotides in length are useful, although longer oligonucleotides of greater than about 25 nucleotides may sometimes be utilized. Some oligonucleotides can be used as “primers” for the synthesis of complimentary nucleic acid strands. For example, DNA primers can hybridize to a complimentary nucleic acid sequence to prime the synthesis of a complimentary DNA strand in reactions using DNA polymerases. Oligonucleotides are also useful for hybridization in several methods of nucleic acid detection, for example, in Northern blotting or in situ hybridization.

“Recombinant” refers to a nucleic acid, a protein encoded by a nucleic acid, a cell, or a viral particle, that has been modified using molecular biology techniques to something other than its natural state. For example, recombinant cells can contain nucleotide sequence that is not found within the native (non-recombinant) form of the cell or can express native genes that are otherwise abnormally, under-expressed, or not expressed at all. Recombinant cells can also contain genes found in the native form of the cell wherein the genes are modified and re-introduced into the cell by artificial means. The term also encompasses cells that contain an endogenous nucleic acid that has been modified without removing the nucleic acid from the cell; such modifications include those obtained, for example, by gene replacement, and site-specific mutation.

The term “high stringency” as used herein refers to the conditions under which two nucleic acids may be hybridized, and may include, for example, the concentration of salts and/or detergents in a solution, the temperature of a solution that is used during the hybridization of the two nucleic acids and time period of the hybridization. Accordingly, the term “high stringency” as used herein refers to conditions in a solution that are conducive to hybridization of two nucleic acids only where such nucleic acids share a high degree of complementarity. The degree of complementarity may include, but not be limited to, a range of from about 90% to 100%. Thus, “high stringency” conditions may involve, but are not limited to, the use of a varying temperature and a buffer comprising various concentrations of detergents, salts, and divalent cations.

As used herein, “vector” refers to a nucleic acid molecule into which a heterologous nucleic acid can be or is inserted. Some vectors can be introduced into a host cell allowing for replication of the vector or for expression of a protein that is encoded by the vector or construct. Vectors typically have selectable markers, for example, genes that encode proteins allowing for drug resistance, origins of replication sequences, and multiple cloning sites that allow for insertion of a heterologous sequence. Vectors are typically plasmid-based and are designated by a lower case “p” followed by a combination of letters and/or numbers. Starting plasmids disclosed herein are either commercially available, publicly available on an unrestricted basis, or can be constructed from available plasmids by application of procedures known in the art. Many plasmids and other cloning and expression vectors that can be used in accordance with the present invention are well-known and readily available to those of skill in the art. Moreover, those of skill readily may construct any number of other plasmids suitable for use in the invention. The properties, construction and use of such plasmids, as well as other vectors, in the present invention will be readily apparent to those of skill from the present disclosure.

As used herein, “proMMP” is used to mean a protein obtained as a result of expression of the pro form of a matrix metalloproteinase (also known as a matrix metalloprotease). Within the meaning of this term, it will be understood that a proMMP encompasses all proteins encoded by a proMMP gene or cDNA, mutants thereof, including deletions, substitutions, and truncations, as well as modified forms thereof. As used herein, the term “proMMP” also includes partially processed forms of a proMMP that have not yet been completely processed to the active form.

As used herein, the term “homologue of MMP9” or “MMP9 homologue” refers to a molecule that is homologous to human proMMP9 by structure or sequence and has the activity of a matrix metalloprotease (MMP) protein when processed to the active form. Examples of human MMP9 homologues include but are not limited to, human proMMP1, human proMMP2, human proMMP3, human proMMP9, human proMMP13, and proMMPs from other species, including proMMPs with conservative substitutions, additions, deletions or combinations thereof. As a non-limiting example, human proMMP9 comprises SEQ ID NO:12 and variants thereof comprising at least about 70% amino acid sequence identity to SEQ ID NO:12, or preferably 80%, 85%, 90% and 95% sequence identity to SEQ ID NO:12, or more preferably, at least about 95% or more sequence identity to SEQ ID NO:12.

As used herein, the terms “homologous region” and “regions homologous to” refer to regions of a protein that may have different primary amino acid sequences but have similar overall secondary and tertiary structures. Homologous regions contemplated for use in the present invention include, but are not limited to, regions homologous to the allosteric binding site of proMMP9 that includes the region occupied by Phe 107 in the apo form of proMMP9.

As used herein, the term “activation” refers to the processing that occurs to change from an inactive pro form of a matrix metalloproteinase (proMMP) to an active form of a matrix metalloproteinase (MMP).

As used herein, the term “activity” or “active form” refers to an activity exerted by a matrix metalloproteinase (MMP) as determined in vivo or in vitro, according to standard techniques. Examples of such activity include, but are not limited to, direct activity such as catalytic activity or the ability to bind to a ligand or an analog thereof, changes in transcriptional activity or changes in the levels of genes or gene products that are regulated directly or indirectly by MMP activity, changes in enzymatic activity for another protein whose expression may be affected directly or indirectly by MMP activity, or functional changes of cell physiology that result from changes in MMP activity.

As used herein, the term “allosteric” relates to binding at a binding site other than the active site.

As used herein, the term “active site” refers to regions on an active MMP or a structural motif of an active MMP that are directly involved in the catalytic activity of a human MMP or a homolog.

As used herein, the terms “processing inhibitor”, “activation inhibitor”, and “inhibitor of activation” all refer to ligands with the ability to inhibit processing of a proMMP to an active form and thus modulate a measurable amount of MMP activity in vitro or in vivo. Preferred processing inhibitors are small-molecules, preferably less than about 1,000 daltons.

As used herein, the term “small-molecule” refers to any molecule, or chemical entity, with a molecular weight of less than about 1,000 daltons.

As used herein, the term “chemical entity” refers to chemical compounds, complexes of at least two chemical compounds, and fragments of such compounds or complexes. The chemical entity may be, for example, a ligand, a substrate, a nucleotide triphosphate, a nucleotide diphosphate, phosphate, a nucleotide, an agonist, antagonist, inhibitor, antibody, drug, peptide, protein or compound.

As used herein, the term “ligand” refers to any molecule, or chemical entity, which binds with or to a human MMP or proMMP, a subunit of an MMP or proMMP, a domain of an MMP or proMMP, a target structural motif of an MMP or proMMP, or a fragment of an MMP or proMMP. Thus, ligands include, but are not limited to, processing inhibitors that bind to a proMMP and inhibit processing of the proMMP to the active MMP form. Preferred ligands are small-molecules, preferably less than about 1,000 daltons.

As used herein, the terms “apo” and “apo form” when used in reference to a proMMP protein, refer to a proMMP protein that does not have an allosteric processing inhibitor bound in an allosteric binding site.

As used herein the terms “bind”, “binding”, “bond”, “bonded” or “bound” when used in reference to the association of atoms, molecules, or chemical groups, refer to any physical contact or association of two or more atoms, molecules, or chemical groups.

As used herein, the terms “binding site” or “binding pocket” refer to a region of an MMP or proMMP, and a molecular complex comprising a ligand and an MMP or proMMP that, as a result of the primary amino acid sequence of the MMP or proMMP and/or its three-dimensional shape, favourably associates with another chemical entity or compound including ligands, cofactors, inhibitors, or other types of modulators.

As used herein, “target structural motif”, “target motif”, or “domain” refer to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration or electron density map which is formed upon the folding of a proMMP or MMP. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymatic active sites, inhibitor binding sites, allosteric binding sites, structural subdomains, epitopes, functional domains and signal sequences. A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention.

By the term “selecting”, “select”, “selected”, “identifying”, “identify”, or “identified” compounds it is intended to encompass both (a) choosing compounds from a group previously unknown to be modulators of a protein complex or interacting protein members thereof and (b) testing compounds that are known to be capable of binding, or modulating the functions and activities of, a protein complex or interacting protein members thereof. The compounds encompass numerous chemical classes, including but not limited to, small organic or inorganic compounds and natural or synthetic molecules. Preferably, they are small organic compounds, i.e., those having a molecular weight of no greater than about 1,000 daltons.

The term “high-throughput assay” or “high-throughput screening” refers to assay designs that allow easy screening of multiple samples simultaneously and/or in rapid succession, and may include the capacity for robotic manipulation. Another desired feature of high-throughput assays is an assay design that is optimized to reduce reagent usage, or minimize the number of manipulations in order to achieve the analysis desired. Examples of high-throughput assay formats include, but are not limited to, formats that utilize 96-well, 384-well, and 1536-well plates, or “lab on a chip” microchannel chips used for liquid handling experiments. It is well known by those in the art that as miniaturization of plastic molds and liquid handling devices are advanced, or as improved assay devices are designed, greater numbers of samples can be processed using the forms of the present invention. The present invention includes any high-throughput screening method utilized to test new compounds which are identified or designed for their ability to interact with a proMMP. For general information on high-throughput screening see, for example, (Devlin (editor) 1998); and U.S. Pat. No. 5,763,263).

As used herein, the term “atomic coordinates” or “structure coordinates” refers to mathematical coordinates that describe the positions of atoms in crystals of a proMMP or MMP in Protein Data Bank (PDB) format, including X, Y, Z and B, for each atom. The diffraction data obtained from the crystals are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps may be used to establish the positions (i.e. coordinates X, Y and Z) of the individual atoms within the crystal. Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error.

The term “atom type” refers to the chemical element whose coordinates are measured.

The terms “X,” “Y” and “Z” refer to the crystallographically-defined atomic position of the element measured with respect to the chosen crystallographic origin. The term “B” refers to a thermal factor that measures the mean variation of an atom's position with respect to its average position.

As used herein, the term “crystal” refers to any three-dimensional ordered array of molecules that diffracts X-rays.

As used herein, the term “carrier” in a composition refers to a diluent, adjuvant, excipient, or vehicle with which the product is mixed.

As used herein, the term “SAR”, an abbreviation for Structure-Activity Relationships, collectively refers to the structure-activity/structure property relationships pertaining to the relationship(s) between a compound's activity/properties and its chemical structure.

As used herein, the term “molecular structure” refers to the three dimensional arrangement of molecules of a particular compound or complex of molecules (e.g., the three dimensional structure of a complex of a proMMP and an allosteric processing inhibitor

As used herein, the term “molecular modeling” refers to the use of computational methods, preferably computer assisted methods, to draw realistic models of what molecules look like and to make predictions about structure activity relationships of ligands. The methods used in molecular modeling range from molecular graphics to computational chemistry.

As used herein, the term “molecular model” refers to the three dimensional arrangement of the atoms of a molecule connected by covalent bonds or the three dimensional arrangement of the atoms of a complex comprising more than one molecule, e.g., a protein:ligand complex.

As used herein, the term “molecular graphics” refers to three dimensional (3D) representations of the molecules; for instance, a 3D representation produced using computer assisted computational methods.

As used herein, “computer readable medium” refers to any medium, which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage media, and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

As used herein, “recorded” refers to a process for storing information on computer readable media. A skilled artisan can readily adopt any of the presently known methods for recording information on computer readable media to generate manufactures comprising an amino acid sequence and/or atomic coordinate/X-ray diffraction data information of the present invention.

As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the sequence and/or X-ray diffraction data of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate which of the currently available computer-based systems are suitable for use in the present invention. A visualization device, such as a monitor, is optionally provided to visualize structure data.

As stated above, the computer-based systems of the present invention comprise a data storage means having stored therein sequence and/or atomic coordinate/X-ray diffraction data of the present invention and the necessary hardware means and software means for supporting and implementing an analysis means. As used herein, “data storage means” refers to memory which can store sequence or atomic coordinate/X-ray diffraction data of the present invention, or a memory access means which can access manufactures having recorded thereon the sequence or X-ray data of the present invention.

As used herein, “search means” or “analysis means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence or X-ray data stored within the data storage means. Search means are used to identify fragments or regions of a protein which match a particular target sequence or target motif. A variety of known algorithms are disclosed publicly and a variety of commercially available software for conducting search means are and can be used in the computer-based systems of the present invention. A skilled artisan can readily recognize that any one of the available algorithms or implementing software packages for conducting computer analyses can be adapted for use in the present computer-based systems.

As used herein, the term “computational chemistry” refers to calculations of the physical and chemical properties of the molecules.

As used herein, the term “molecular replacement” refers to a method that involves generating a preliminary model of a crystal of a complex of a proMMP and an allosteric processing inhibitor whose coordinates are unknown, by orienting and positioning the said atomic coordinates described in the present invention so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. (Rossmann 1972)

As used herein, the term “homolog” refers to a proMMP molecule or the nucleic acid molecule which encodes the protein, or a functional domain from said protein from a first source having at least about 70% or 75% sequence identity, or at least about 80% sequence identity, or more preferably at least about 85% sequence identity, or even more preferably at least about 90% sequence identity, and most preferably at least about 95%, 97% or 99% amino acid or nucleotide sequence identity, with the protein, encoding nucleic acid molecule or any functional domain thereof, from a second source. The second source may be a version of the molecule from the first source that has been genetically altered by any available means to change the primary amino acid or nucleotide sequence or may be from the same or a different species than that of the first source.

The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean.

As used herein, the term “hydrogen bond” refers to two hydrophilic atoms (either O or N), which share a hydrogen that is covalently bonded to only one atom, while interacting with the other.

As used herein, the term “hydrophobic interaction” refers to interactions made by two hydrophobic residues or atoms (such as Carbon).

As used herein, the term “conjugated system” refers to more than two double bonds adjacent to each other, in which electrons are completely delocalized with the entire system. This also includes aromatic residues.

As used herein, the term “aromatic residue” refers to amino acids with side chains having a delocalized conjugated system. Examples of aromatic residues are phenylalanine, tryptophan, and tyrosine.

As used herein, the term “R or S-isomer” refers to two possible stereoisomers of a chiral carbon according to the Cahn-Ingold-Prelog system adopted by International Union of Pure and Applied Chemistry (IUPAC). Each group attached to the chiral carbon is first assigned to a preference or priority a, b, c, or d on the basis of the atomic number of the atom that is directly attached to the chiral carbon. The group with the highest atomic number is given the highest preference a, the group with next highest atomic number is given the next highest preference b, and so on. The group with the lowest preference (d) is then directed away from the viewer. If the trace of a path from a to b to c is counter clockwise, the isomer is designated (S); in the opposite direction, clockwise, the isomer is designated (R).

As used herein, the term “stereoisomers” is a general term for all isomers of individual molecules that differ only in the orientation of their atoms in space. It includes enantiomers and isomers of compounds with more than one chiral center that are not mirror images of one another (diastereomers).

As used herein, the term “chiral center” refers to a carbon atom to which four different groups are attached.

As used herein, the term “enantiomer” or “enantiomeric” refers to a molecule that is nonsuperimposable on its mirror image and hence optically active wherein the enantiomer rotates the plane of polarized light in one direction and its mirror image rotates the plane of polarized light in the opposite direction.

As used herein, the term “racemic” refers to a mixture of equal parts of enantiomers and which is optically active.

As used herein, the term “resolution” refers to the separation or concentration or depletion of one of the two enantiomeric forms of a molecule. In the context of this application. The term “resolution” also refers to the amount of detail, which can be resolved by the diffraction experiment. Or in other terms, since the inherent disorder of a protein crystal diffraction pattern fades away at some diffraction angle theta_(max), the corresponding distance d_(min), of the reciprocal lattices is determined by Bragg's law. In practice in protein crystallography it is usual to quote the nominal resolution of a protein electron density in terms of d_(min), the minimum lattice distance to which data is included in the calculation of the map.

As used herein, the terms “covalent bond” or “valence bond” refer to a chemical bond between two atoms in a molecule created by the sharing of electrons, usually in pairs, by the bonded atoms.

As used herein, “noncovalent bond” refers to an interaction between atoms and/or molecules that does not involve the formation of a covalent bond between them.

The term “composition” is intended to encompass a product comprising the specified ingredients in the specified amounts, as well as any product which results, directly or indirectly, from combinations of the specified ingredients in the specified amounts. For the purposes of this invention, a composition will often, but not always comprise a carrier.

The term “subject” as used herein, refers to an animal, preferably a mammal, most preferably a human, who is the object of treatment, observation or experiment.

Methods are known in the art for determining effective doses for therapeutic and prophylactic purposes for the disclosed pharmaceutical compositions or the disclosed drug combinations, whether or not formulated in the same composition. For therapeutic purposes, the term “therapeutically effective amount” as used herein, means that amount of each active compound or pharmaceutical agent, alone or in combination, that elicits the biological or medicinal response in a tissue system, animal or human that is being sought by a researcher, veterinarian, medical doctor or other clinician, which includes alleviation of the symptoms of the disease or disorder being treated. For prophylactic purposes (i.e., inhibiting the onset or progression of a disorder), the term “therapeutically effective amount” refers to that amount of each active compound or pharmaceutical agent, alone or in combination, that treats or inhibits in a subject the onset or progression of a disorder as being sought by a researcher, veterinarian, medical doctor or other clinician. Thus, the present invention provides combinations of two or more drugs wherein, for example, (a) each drug is administered in an independently therapeutically or prophylactically effective amount; (b) at least one drug in the combination is administered in an amount that is sub-therapeutic or sub-prophylactic if administered alone, but is therapeutic or prophylactic when administered in combination with the second or additional drugs according to the invention; or (c) both (or more) drugs are administered in an amount that is sub-therapeutic or sub-prophylactic if administered alone, but are therapeutic or prophylactic when administered together.

The term “pharmaceutically acceptable salt” refers to non-toxic pharmaceutically acceptable salts (Berge, Bighley et al. 1977; Gould 1986). Other salts well known to those in the art may, however, be useful in the preparation of compounds according to this invention or of their pharmaceutically acceptable salts. Representative organic or inorganic acids include, but are not limited to, hydrochloric, hydrobromic, hydriodic, perchloric, sulfuric, nitric, phosphoric, acetic, propionic, glycolic, lactic, succinic, maleic, fumaric, malic, tartaric, citric, benzoic, mandelic, methanesulfonic, hydroxyethanesulfonic, benzenesulfonic, oxalic, pamoic, 2-naphthalenesulfonic, p-toluenesulfonic, cyclohexanesulfamic, salicylic, saccharinic or trifluoroacetic acid. Representative organic or inorganic bases include, but are not limited to, basic or cationic salts such as benzathine, chloroprocaine, choline, diethanolamine, ethylenediamine, meglumine, procaine, aluminum, calcium, lithium, magnesium, potassium, sodium and zinc.

DETAILED DESCRIPTION OF ILLUSTRATIVE EMBODIMENTS

It is to be understood at the outset, that the figures and examples provided herein are to exemplify, and not to limit the invention and its various embodiments.

The present invention includes a crystal comprising a complex of a proMMP and an allosteric processing inhibitor that inhibits that activation of the proMMP, methods for identifying allosteric processing inhibitors that inhibit the activation of proMMPs, and methods of inhibiting the activation of proMMPs with allosteric processing inhibitors. In a non-limiting example, the proMMP is human proMMP9 and the allosteric processing inhibitor is a small-molecule with a molecular weight of no greater than about 1,000 daltons.

Engineered Forms and Fragments

Engineered forms of a proMMP or fragments thereof, for instance engineered forms or fragments comprising the pro domain defined by two or more amino acids may be prepared by any available means including synthetic or recombinant means. Such fragments may then be used in the assays as described herein, for example, but not limited to, high-throughput assays to detect interactions between prospective ligands and the pro domain within the fragment.

For recombinant expression or production of the forms or fragments of the invention, nucleic acid molecules encoding the form or fragment may be prepared. Nucleic acid molecules encoding engineered forms or fragments of the invention may differ in sequence because of the degeneracy in the genetic code or may differ in sequence as they encode proteins or protein fragments that differ in amino acid sequence. Homology or sequence identity between two or more such nucleic acid molecules is determined by BLAST (Basic Local Alignment Search Tool) analysis using the algorithm employed by the programs blastp, blastn, blastx, tblastn and tblastx (Karlin and Altschul 1990) and (Altschul 1993), which are tailored for sequence similarity searching.

The approach used by the BLAST program is to first consider similar segments between a query sequence and a database sequence, then to evaluate the statistical significance of all matches that are identified and finally to summarize only those matches which satisfy a preselected threshold of significance. For a discussion of basic issues in similarity searching of sequence databases, see (Altschul, Boguski et al. 1994). The search parameters for histogram, descriptions, alignments, expect (i.e., the statistical significance threshold for reporting matches against database sequences), cutoff, matrix and filter are at the default settings. For a discussion of default scoring matrix used by blastp, blastx, tblastn, and tblastx, see (Henikoff 1992).

The encoding nucleic acid molecules of the present invention or fragments thereof (i.e., synthetic oligonucleotides) and those that are used as probes or specific primers for polymerase chain reaction (PCR) or to synthesize gene sequences encoding proteins of the invention can easily be synthesized by chemical techniques, for example, the phosphotriester method of (Matteucci and Caruthers 1981) or using automated synthesis methods. In addition, larger DNA segments can readily be prepared by well-known methods, such as synthesis of a group of oligonucleotides that define various modular segments of the gene, followed by ligation of oligonucleotides to build the complete modified gene.

The encoding nucleic acid molecules of the present invention may further be modified so as to contain a detectable label for diagnostic and probe purposes. There are a variety of such labels known in the art that can readily be employed with the encoding molecules herein described. Suitable labels include, but are not limited to, biotin, radiolabeled nucleotides and the like. A skilled artisan can employ any of the art-known labels to obtain a labeled encoding nucleic acid molecule.

The present invention further provides recombinant DNA molecules (rDNA) that contain a coding sequence for a protein or protein fragment as described herein. As used herein, an rDNA molecule is a DNA molecule that has been subjected to molecular manipulation. Methods for generating rDNA molecules are well known in the art, for example, see (Sambrook, Fritsch et al. 1989). In the preferred rDNA molecules, a coding DNA sequence is operably linked to expression control sequences and/or vector sequences.

The choice of vector and expression control sequences to which one of the protein encoding sequences of the present invention is operably linked depends directly, as is well known in the art, on the functional properties desired (e.g., protein expression, and the host cell to be transformed). A vector of the present invention may be capable of directing the replication or insertion into the host chromosome, and preferably also expression, of the structural gene included in the rDNA molecule.

Expression control elements that are used for regulating the expression of an operably linked protein encoding sequence are known in the art and include, but are not limited to, inducible promoters, constitutive promoters, secretion signals, and other regulatory elements. Preferably, the inducible promoter is readily controlled, such as being responsive to a nutrient in the host cell's medium.

The present invention further provides host cells transformed with a nucleic acid molecule that encodes a protein or protein fragment of the present invention. The host cell can be either prokaryotic or eukaryotic. Eukaryotic cells useful for expression of a protein of the invention are not limited, so long as the cell line is compatible with cell culture methods and compatible with the propagation of the expression vector and expression of the gene product. Preferred eukaryotic host cells include, but are not limited to, insect, yeast, and mammalian cells. Preferred eukaryotic host cells include Spodoptera frugiperda (Sf9 or Sf21) insect cells and human embryonic kidney cells (HEK cells).

Transformed host cells of the invention may be cultured under conditions that allow the production of the recombinant protein. Optionally the recombinant protein is isolated from the medium or from the cells; recovery and purification of the protein may not be necessary in some instances where some impurities may be tolerated.

Kits may also be prepared with any of the described nucleic acid molecules, proteins, protein fragments, vector and/or host cells optionally packaged with the reagents needed for a specific assay. In such kits, the protein, protein fragments, or other reagents may be attached to a solid support, such as glass or plastic beads.

High-Throughput Assays

Compound identification methods can be performed using conventional laboratory assay formats or in high-throughput assays, including, but not limited to, those described below.

Immunoassays

Immunoassays are a group of techniques used for the measurement of specific biochemical substances, commonly at low concentrations in complex mixtures such as biological fluids. The assays depend upon suitably prepared and selected antibodies with specificity and high affinity for their complementary antigens. A substance to be measured must, of necessity, be antigenic, either an immunogenic macromolecule or a haptenic small-molecule. To each sample a known limited amount of specific antibody is added and the fraction of the antigen combining with it, often expressed as the bound:free ratio, is estimated by quantifying the signal from the antibody. Quantification can be achieved with a number of readily identifiable labels and used for various types of assays, including, but not limited to, radioisotopes for radioimmunoassays (RIA), fluorescent molecules for fluoroimmunoassays (FIA), stable free radicals for spin immunoassays, chemiluminescent molecules for chemiluminescent immunoassays (CLIA), colloidal gold particles for immunogold assays, and enzymes for enzyme-linked immunosorbent assays (ELISA).

A common immunoassay format is the ELISA, which avoids the hazards of radiochemicals and the expense of fluorescence detection systems. Instead, an ELISA is a form of quantitative immunoassay based on the use of antibodies (or antigens) that may be linked to an insoluble carrier surface, which is then used to “capture” the relevant antigen (or antibody) in the test solution. The antigen-antibody complex is then detected by measuring the activity of an appropriate enzyme that can be covalently attached to the capture antigen (or antibody) or to a subsequent “detection” antibody (or antigen). For more information on ELISA techniques, see, for example, (Crowther 1995); (Kemeny (editor) and Challacombe (editor) 1988), (Kemeny 1991), and (Ishikawa 1999).

Colorimetric Assays

Colorimetric assays for enzymes are methods of quantitative chemical analysis in which the concentration or amount of a compound is determined by comparing the color produced by the reaction of a reagent with both standard and test amounts of the compound, often using a colorimeter. A colorimeter is a device for measuring color intensity or differences in color intensity, either visually or photoelectrically. For example, standard colorimetric assays of beta-galactosidase enzymatic activity are well known to those skilled in the art, see e.g., (Norton and Coffin 1985). A colorimetric assay can be performed with purified components or on whole cell lysates, using for example, O-nitrophenyl-beta-D-galacto-pyranoside (ONPG, Sigma) as the substrate in a standard colorimetric beta-galactosidase assay (Sambrook, Fritsch et al. 1989). Automated colorimetric assays are also available, see for example, detection of beta-galactosidase activity as described in U.S. Pat. No. 5,733,720.

Fluorescence Assays

Enzymatic substrates that become fluorescent after being acted upon by an enzyme generally are well known. Such fluorescent substrates typically have two components that are bound to one another through, for example, a covalent chemical bond. One component is a fluorescent molecule that is capable of fluorescing by first accepting light energy and then emitting light energy. The other component is an entity that prevents the fluorescent molecule from accepting or emitting light energy when the two components are covalently bound to one another. In the presence of an appropriate enzyme, the enzyme cleaves the covalent bond between the two components and separates one component from the other to permit the fluorescent molecule to accept and emit light energy. In other words, the enzyme frees the fluorescent molecule and allows it to fluoresce. Ideally, fluorescent substrates should be soluble and stable in aqueous buffers, should have a high affinity for the enzymes that act upon them, and should yield a strong signal upon enzymatic action (U.S. Pat. No. 5,998,593A).

Detecting fluorescence emitted from the fluorescent component of a fluorescent enzyme substrate is typically achieved in two steps. The fluorescent molecule is first excited with light energy and subsequently the fluorescence emitted from the fluorescent component is then detected. Generally, fluorescent molecules can be excited with light energy from, for example, a laser or another suitable light source. Fluorescence is detected with a device designed to detect light energy of a wavelength that is emitted by the fluorescent molecule. Such excitation and emission detection systems generally are designed to operate at particular wavelength ranges (U.S. Pat. No. 5,998,593A).

Time-resolved Fluorescence resonance energy transfer (TR-FRET) unites TRF (Time-Resolved Fluorescence) and FRET (Fluorescence Resonance Energy Transfer) principles. This combination brings together the low background benefits of TRF with the homogeneous assay format of FRET. Time-resolved fluorometry (TRF) takes advantage of the unique properties of the rare earth elements called lanthanides. Specifically, lanthanides have large Stoke's shifts and extremely long emission half-lives compared to more traditional fluorophores. The commonly used lanthanides in TRF assays are samarium (Sm), europium (Eu), terbium (Tb), and dysprosium (Dy). Lanthanides are complexed with organic moieties that harvest light and transfer it to the lanthanide through intramolecular processes. FRET uses two fluorophores, a donor and an acceptor. Excitation of the donor by an energy source (e.g. flash lamp or fluorometer laser) triggers an energy transfer to the acceptor if they are within a given proximity to each other. The acceptor in turn emits light at its given wavelength. Because of this energy transfer, molecular interactions between biomolecules can be assessed by coupling each partner with a fluorescent label and detecting the level of energy transfer. More importantly acceptor emissions, as a measure of energy transfer, can be detected without the need to separate bound from unbound assay components (Klostermeier and Millar 2001).

Thermofluor® Assays

ThermoFluor® assays are based on a classical method for estimating ligand binding affinities, by measuring the effect of a ligand on stability using chemical or thermal denaturation methods (Pantoliano, Petrella et al. 2001). This approach is general, applicable to a wide variety of systems, and rigorous in theoretical interpretation through quantitation of equilibrium binding constants (i.e. true K_(D) values). The technique monitors changes in the fluorescent intensity of dyes such as 1-anilinonaphthalene-8-sulfonic acid (1,8-ANS). The fluorescent dyes are quenched in aqueous environments but increase in fluorescence on binding to the hydrophobic core of denatured proteins.

In an experiment where stability is monitored as the temperature is steadily increased, either kinetic or equilibrium theory would dictate that equilibrium binding ligands would cause the midpoint of an unfolding transition to occur at a higher temperature, described as a ΔT_(m). The dependence of ΔT_(m) on added ligand is a function of the equilibrium constant for both ligand binding and protein stability. In addition, the results of compound binding may be compared based on the magnitude of ΔT_(m) at a fixed, single concentration of ligand, as the contribution of binding energy to protein stability is determined by the product of the binding constant and ligand concentration. Thus, compound potency may be compared as a rank order of either ΔT_(m) values (“screening” mode) or in terms of K_(D) values (complete concentration response curves). The dynamic range of measurable K_(D) values spans ˜200 uM to <10 pM; resolution is limited only be the upper limit on ligand solubility.

Homogenous, 384-well plate-based assays run in a Thermofluor® instrument, were developed by 3-Dimensional Pharmaceuticals (Pantoliano, Petrella et al. 2001; Matulis, Kranz et al. 2005). Assay components typically include a protein (1-5 μM) with dye (25-100 μM, typically 1,8-ANS or dapoxylsulfonamide) in buffer, with or without ligand. Assay volumes are typically 2-4 uL with 1 uL silicone oil overlay to limit evaporation, dispensed into an appropriate 384-well thermocycler assay plate. The assay measures dye fluorescence on a plate-basis via CCD camera, ramping temperature of the 384-well plate from ambient to high temperature, imaging the change in dye fluorescence upon increasing the temperature incrementally. Protein unfolding energetics and ligand binding energetics are quantitated based on proven biophysical principles.

Modeling the Three-Dimensional Structure

The atomic coordinate data provided herein, or the coordinate data derived from homologous proteins may be used to build a three-dimensional model of a complex of a proMMP and an allosteric processing inhibitor that inhibits the activation of a proMMP. Any available computational methods may be used to build the three dimensional model. As a starting point, the X-ray diffraction pattern obtained from the assemblage of the molecules or atoms in a crystalline version of a proMMP or a proMMP homolog can be used to build an electron density map using tools well known to those skilled in the art of crystallography and X-ray diffraction techniques. Additional phase information extracted either from the diffraction data and available in the published literature and/or from supplementing experiments may then be used to complete the reconstruction.

For basic concepts and procedures of collecting, analyzing, and utilizing X-ray diffraction data for the construction of electron densities see, for example, (Campbell 1984), (Cantor and Schimmel 1980), (Brunger 1993), (Woolfson 1997), (Drenth 1999), (Tsirelson and Ozerov 1996), and (U.S. Pat. No. 5,942,428A); (U.S. Pat. No. 6,037,117A); (U.S. Pat. No. 5,200,910A); and (U.S. Pat. No. 5,365,456A).

For basic information on molecular modeling, see, for example, (Schlecht 1998); (Gans, Amann et al. 1996); (Cohen (editor) 1996); and (Smith 1996). U.S. Patents which provide detailed information on molecular modeling include (U.S. Pat. No. 4,906,122A; U.S. Pat. No. 5,030,103A; U.S. Pat. No. 5,583,973A; U.S. Pat. No. 5,612,894A; U.S. Pat. No. 5,994,503A; U.S. Pat. No. 6,071,700A; U.S. Pat. No. 6,075,014A; U.S. Pat. No. 6,075,123A; U.S. Pat. No. 6,080,576A; U.S. Pat. No. 6,093,573A).

Methods of Using the Atomic Coordinates to Identify and Design Ligands

The atomic coordinates described herein, or coordinates substantially identical to or homologous to those described herein may be used with any available methods to prepare three dimensional models of a complex of a proMMP and an allosteric processing inhibitor that inhibits the activation of a proMMP, as well as to identify and design allosteric processing inhibitors that inhibit the activation of a proMMP. Such methods provide the amino acid sequence and/or X-ray diffraction data in a form which allows a skilled artisan to analyze and molecular model the three-dimensional structure of a complex of a proMMP and an allosteric processing inhibitor that inhibits the activation of a proMMP or related molecules, including a subdomain thereof.

For instance, three-dimensional modeling may be performed using the experimentally determined coordinates derived from X-ray diffraction patterns, such as those described herein. For example, wherein such modeling includes, but is not limited to, drawing pictures of the actual structures, building physical models of the actual structures, and determining the structures of related subunits and proMMP:ligand and proMMP subunit:ligand complexes using the coordinates. Such molecular modeling can utilize known X-ray diffraction molecular modeling algorithms or molecular modeling software to generate atomic coordinates corresponding to the three-dimensional structure of a complex of a proMMP and a ligand that inhibits the activation of a proMMP.

As described above, molecular modeling involves the use of computational methods, preferably computer assisted methods, to build realistic models of molecules that are identifiably related in sequence to the known crystal structure. It also involves modeling new small-molecules bound to a proMMP starting with the structures of a proMMP and or a proMMP complexed with known ligands or other molecules. The methods utilized in ligand modeling range from molecular graphics (i.e., 3D representations) to computational chemistry (i.e., calculations of the physical and chemical properties) to make predictions about the binding of ligands or activities of ligands; to design new ligands; and to predict novel molecules, including ligands such as drugs, for chemical synthesis, collectively referred to as rational drug design.

One approach to rational drug design is to search for known molecular structures that might bind to an active site or allosteric binding site. Using molecular modeling, rational drug design programs can look at a range of different molecular structures of drugs that may fit into the site, and by moving them in a three-dimensional environment it can be decided which structures actually fit the site well.

An alternative but related rational drug design approach starts with the known structure of a complex with a small-molecule ligand and models modifications of that small-molecule in an effort to make additional favourable interactions with a proMMP.

The present invention includes the use of molecular and computer modeling techniques to design and select ligands, such as small-molecule ligands that act as allosteric processing inhibitors of a proMMP. For example, the invention as herein described includes the design of ligands that bind a proMMP and inhibit processing of the proMMP to a catalytically active form of the protein. In a preferred, but non limiting embodiment, the ligands bind to proMMP9 and inhibit processing of proMMP9 to the catalytically active form of MMP9. In another nonlimiting embodiment, the present invention provides a method to design allosteric processing inhibitors using the atomic coordinates of a complex of proMMP9 and an allosteric processing inhibitor of the present invention.

The atomic coordinates of the present invention also provide the needed information to probe a crystal of a proMMP with different molecules composed of a variety of different chemical features to determine optimal sites of interaction on the proMMP to identify potential allosteric processing inhibitors of a proMMP. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of where each type of solvent molecule sticks. Small molecules that bind to those sites can then be designed and synthesized and tested for their ability to modulate activity (Travis 1993).

The present invention also includes methods for computationally screening small-molecule databases and libraries for chemical entities, agents, ligands, or compounds that can bind in whole, or in part, to a proMMP. In this screening, the quality of fit of such entities or compounds to the binding site or sites may be judged either by shape complementarity or by estimated interaction energy (Meng, Shoichet et al. 1992).

The design of ligands that bind to or inhibit the activation of a proMMP according to this invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with a proMMP. In addition to the covalent interaction described herein, non-covalent molecular interactions important in the association of a proMMP with the ligand include hydrogen bonding, van der Waals and hydrophobic interactions. Second, the ligand must be able to assume a conformation that allows it to associate with a proMMP. Although certain portions of the ligand may not directly participate in the association with a proMMP, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on binding affinities, therapeutic efficacy, drug-like qualities and potency of the ligand. Such conformational requirements include the overall three-dimensional structure and orientation of the ligand in relation to all or a portion of the binding site or other region of the proMMP, or the spacing between functional groups of a ligand comprising several chemical entities that directly interact with the proMMP.

The potential or predicted ability of a ligand to bind to a proMMP and inhibit activation of the proMMP may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given ligand suggests insufficient interaction and association between it and a proMMP, synthesis and testing of the ligand may be obviated. If computer modeling indicates a strong interaction, however, the molecule may then be synthesized and tested for its ability to interact with a proMMP. In this manner, synthesis of inoperative ligands may be avoided. In other cases, inactive ligands can be synthesized based on modeling and then tested to help develop SAR (structure-activity relationship) that can be used to design other compounds that interact with a specific region of a proMMP.

One skilled in the art may use one of several methods to screen chemical entities, fragments, compounds, or other agents for use as ligands based on their ability to associate with a proMMP and more particularly their ability to associate with the individual binding pocket of a proMMP as described in the present invention. In a nonlimiting example, the proMMP is human proMMP9. This process may begin by visual inspection of, for example, the allosteric binding site on the computer screen based on the atomic coordinates of a proMMP or a proMMP complexed with a ligand. Selected chemical entities, compounds, or agents may then be positioned in a variety of orientations, or docked within an individual binding pocket of a proMMP. Docking may be accomplished using software such as, but not limited to, QUANTA, available from Accelrys, Inc., San Diego, Calif.; and SYBYL, available for Tripos, St. Louis, Mo.; followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMm; available from Accelrys, Inc., San Diego, Calif.; and AMBER, University of California, San Francisco.

Specialized computer programs may also assist in the process of selecting chemical entities. These include but are not limited to: GRID (Goodford 1985), available from Oxford University, Oxford, UK); MCSS (Miranker and Karplus 1991), available from Molecular Simulations, Burlington, Mass.; AUTODOCK (Goodsell and Olsen 1990), available from Scripps Research Institute, La Jolla, Calif.; and DOCK (Kuntz, Blaney et al. 1982), available from University of California, San Francisco, Calif.

The use of software such as GRID, a program that determines probable interaction sites between probes with various functional group characteristics and the macromolecular surface, is used to analyze the surface sites to determine structures of similar inhibiting proteins or compounds. The GRID calculations, with suitable inhibiting groups on molecules (e.g., protonated primary amines) as the probe, are used to identify potential hotspots around accessible positions at suitable energy contour levels. The program DOCK may be used to analyze an active site or ligand-binding site and suggest ligands with complementary steric properties.

Once suitable chemical entities, compounds, or agents have been selected as potential ligands, they can be assembled into a single ligand, compound, antagonist (inhibitor), agonist (activator), or inverse agonist. Assembly may proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image. This may be followed by manual model building using software such as QUANTA or SYBYL.

Useful programs to aid in connecting the individual chemical entities, compounds, or agents include but are not limited to: CAVEAT (Bartlett, Shea et al. 1989); 3D Database systems such as MACCS-3D (Martin 1992), available from MDL Information Systems, San Leandro, Calif.; and HOOK, available from Molecular Simulations, Burlington, Mass.

Several methodologies for searching three-dimensional databases to test pharmacophore hypotheses and select compounds for screening are available. These include the program CAVEAT (Bacon and Moult 1992). For instance, CAVEAT uses databases of cyclic compounds which can act as “spacers” to connect any number of chemical fragments already positioned in the active site. This allows one skilled in the art to quickly generate hundreds of possible ways to connect the fragments already known or suspected to be necessary for tight binding.

Instead of proceeding to build an allosteric processing inhibitor of a proMMP in a step-wise fashion, one chemical entity at a time as described above, such ligands may be designed as a whole or “de novo” using either an empty binding site or optionally including some portion(s) of a known molecule(s). These methods include: LUDI (Bohm 1992), available from Biosym Technologies, San Diego, Calif.; LEGEND (Nishibata and Itai 1991), available from Molecular Simulations, Burlington, Mass.; and LeapFrog, available from Tripos Associates, St. Louis, Mo., USA.

For example, the program LUDI can determine a list of interaction sites into which to place both hydrogen bonding and hydrophobic fragments. LUDI then uses a library of linkers to connect up to four different interaction sites into fragments. Then smaller “bridging” groups such as —CH₂— and —COO— are used to connect these fragments. For the enzyme DHFR, the placements of key functional groups in the well-known inhibitor methotrexate were reproduced by LUDI. See also, (Rotstein and Murcko 1993).

Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., (Cohen, Blaney et al. 1990). See also, (Navia and Murcko 1992).

Once a ligand has been designed or selected by the above methods, the affinity with which that ligand may bind or associate with a proMMP may be tested and optimized by computational evaluation and/or by testing biological activity after synthesizing the compound. Ligands may interact with the proMMP in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free ligand and the average energy of the conformations observed when the ligand binds to the proMMP.

A ligand designed or selected as binding or associating with a proMMP may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the proMMP. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the compound and the proMMP when the compound is bound, preferably make a neutral or favourable contribution to the enthalpy of binding. Weak binding compounds will also be designed by these methods so as to determine SAR.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (Frisch, Trucks et al. 1992); AMBER, University of California, San Francisco; QUANTA and CHARMm, available from Accelrys, Inc., San Diego, Calif.; and Insight II/Discover, from Biosysm Technologies Inc., San Diego, Calif., USA. Other hardware systems and software packages will be known to those skilled in the art.

Once a ligand that associates with a proMMP has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation may be avoided. Such substituted ligands may then be analyzed for efficiency of fit to the proMMP by the same computer methods described in detail above.

Use of Homology Structure Modeling to Design Ligands

The present invention includes the use of the atomic coordinates and structures of a proMMP and a proMMP complexed with an allosteric processing inhibitor to design modifications to starting ligands and derivatives thereof that will bind more tightly or interact more specifically to a proMMP or other related proMMP proteins to design an allosteric processing inhibitor. The structure of the complex between proMMP and the starting ligand can be used to guide the modification of that ligand to produce new ligands that have other desirable properties for applicable industrial and other uses (e.g., as pharmaceuticals), such as chemical stability, solubility or membrane permeability. (Lipinski, Lombardo et al. 1997).

Ligands known and unknown in the art can be diffused into or soaked with the stabilized crystals of a proMMP to form a complex for collecting X-ray diffraction data. Alternatively, ligands known and unknown in the art can be cocrystallized with a proMMP, by mixing the ligand with the proMMP before crystallization. In a nonlimiting example, the proMMP is human proMMP9.

To produce custom high affinity and very specific compounds, the structure of the present invention of human proMMP9 complexed with an allosteric processing inhibitor can be compared to the structure of a selected non-targeted proMMP molecule and a hybrid structure can be constructed by changing the structure of the non-targeted proMMP molecule to include structural features described at the allosteric binding site provided in the present invention. The process whereby this modeling is achieved is referred to as homology structure modeling. This can be done computationally by removing the side chains from the known structure of the present invention and systematically replacing them with the chains of the non-targeted proMMP molecule, such that the side chains are placed in sterically plausible positions. In this way it can be understood how the shapes of the binding site cavities of the targeted and non-targeted molecules differ. This process, therefore, provides information concerning how a bound ligand can be chemically altered in order to produce compounds that will bind tightly and specifically to the desired target but will simultaneously be sterically prevented from binding to the non-targeted molecule. Likewise, knowledge of portions of the bound ligands that are facing to the solvent allows introduction of other functional groups for additional pharmaceutical purposes. The use of homology structure modeling to design ligands that bind more tightly to the target enzyme than to the non-target enzyme has wide spread applicability. In particular, in a non-limiting example, homology structure modeling has applicability to designing compounds with high specificity for a targeted proMMP such as human proMMP9.

Databases and Computer Systems

An amino acid sequence or nucleotide sequence of a proMMP and/or X-ray diffraction data, useful for computer molecular modeling of the proMMP or a portion thereof, can be provided in a variety of mediums to facilitate use thereof. In one application of this embodiment, databases comprising data pertaining to X-ray diffraction data for a complex of a proMMP and an allosteric processing inhibitor, or at least one proMMP subdomain thereof, is recorded on computer readable medium. A skilled artisan can readily appreciate how any of the presently known computer readable media can be used to create a manufacture comprising computer readable medium having recorded thereon data pertaining to X-ray diffraction data of the present invention.

A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon an amino acid sequence and/or atomic coordinate/X-ray diffraction data of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the sequence and X-ray data information of the present invention on computer readable media. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and MICROSOFT Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A skilled artisan can readily adapt any number of data processor structuring formats (e.g., text file or database) in order to obtain computer readable media having recorded thereon the information of the present invention.

By providing computer readable media having sequence and/or atomic coordinates based on X-ray diffraction data, a skilled artisan can routinely access the sequence and atomic coordinates or X-ray diffraction data to model a related molecule, a subdomain, mimetic, or a ligand thereof. Computer algorithms are publicly and commercially available which allow a skilled artisan to access this data provided in a computer readable medium and analyze it for molecular modeling and/or RDD (rational drug design). See, e.g., (Mary Ann Liebert (Publishers) 1995).

The present invention further provides systems, particularly computer-based systems, which contain the sequence and/or diffraction data described herein. Such systems are designed to do structure determination and rational drug design (RDD) using information such as a complex of a ligand that inhibits the activation of the proMMP and a proMMP, or at least one subdomain thereof. Non-limiting examples are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running UNIX based software, Windows NT or IBM OS/2 operating systems.

A variety of comparing means can also be used to compare a target sequence or target motif with the data storage means to identify structural motifs or electron density maps derived in part from the atomic coordinate/X-ray diffraction data. A skilled artisan can readily recognize that any one of the publicly available computer modeling programs can be used as the search means for the computer-based systems of the present invention.

Integrated Procedures Which Utilize the Present Invention

Molecular modeling is provided by the present invention for rational drug design (RDD) of ligands that inhibit the activation of a proMMP. As described above, the drug design paradigm uses computer-modeling programs to determine potential ligands which are expected to interact with sites on the protein. The potential ligands are then screened for activity and/or binding and/or interaction. For proMMP related ligands, screening methods can be selected from an assay of at least one biological activity of an MMP.

Thus, the tools and methodologies provided by the present invention may be used in procedures for identifying and designing ligands which bind in desirable ways with the target. Such procedures utilize an iterative process whereby ligands are synthesized, tested and characterized. New ligands can be designed based on the information gained in the testing and characterization of the initial ligands and then such newly identified ligands can themselves be tested and characterized. This series of processes may be repeated as many times as necessary to obtain ligands with the desirable binding properties.

It is to be understood that the present invention is considered to include stereoisomers as well as optical isomers, e.g., mixtures of enantiomers as well as individual enantiomers and diastereomers, which arise as a consequence of structural asymmetry in selected compounds of the present invention.

Some of the ligands disclosed or discovered by the methods herein may contain one or more asymmetric centers and thus give rise to enantiomers, diastereomers, and other stereoisomeric forms. The present invention is also meant to encompass all such possible forms as well as their racemic and resolved forms and mixtures thereof. When the ligands described or discovered herein contain olefinic double bonds or other centers of geometric asymmetry, and unless otherwise specified, it is intended to include both E and Z geometric isomers. All tautomers are intended to be encompassed by the present invention as well.

EXAMPLES

Without further description, it is believed that one of ordinary skill in the art can, using the preceding description and the following illustrative examples, make and utilize the present invention and practice the claimed methods. The following working examples therefore, specifically point out preferred embodiments of the present invention, and are not to be construed as limiting in any way the remainder of the disclosure.

Example Compounds Example 1 N-[2-(2-Methoxy-phenylamino)-4′-methyl-[4,5′]bithiazolyl-2′-yl]-acetamide)

Example 1 is a commercially available compound from ChemBridge.

Example 2 3-(2′,4′-Dimethyl-[4,5′]bithiazolyl-2-ylamino)-4-isopropoxy-benzenesulfonamide.HBr

Example 2 step a 2-Bromo-1-(2,4-dimethyl-thiazol-5-yl)-ethanone.HBr

A suspension of bromine (11.9 mL, 231.5 mmol) in 1,4-dioxane (200 mL) was added to a stirred solution of 1-(2,4-dimethyl-thiazol-5-yl)-ethanone (28.75 g, 185.2 mmol, Alfa) in 1,4-dioxane (200 mL). The mixture was stirred for 25 h at 50° C. and the resulting cream-colored suspension was allowed to cool to room temperature and was filtered and washed with 2:1 heptane:EtOAc (v/v). The resulting white powder was recrystallized from EtOH, affording the title compound.

Example 2 step b 4-Fluoro-3-nitro-benzenesulfonamide

Following the procedure of J. Med. Chem. 2006, 49, 1173, a solution of commercially available 2-fluoronitrobenzene (10.00 g, 70.87 mmol) and chlorosulfonic acid (21 mL) were heated to reflux for 18 hours at 95° C. and then cooled to room temperature. The solution was then added dropwise over a 1 hour period to a solution of iPrOH (225 mL) and concentrated aqueous NH₄OH (54 mL) at −35° C. and stirred for 0.5 hours. The solution was maintained at −35° C. while concentrated aqueous HCl was added until the pH was acidic. The solution was then evaporated to remove some iPrOH, water was added and the solution was evaporated again to remove most of the iPrOH. More water was added, the solution was filtered and the solid was washed with 1 N aqueous HCl and water to give the title compound.

Example 2 Step c 4-Isopropoxy-3-nitro-benzenesulfonamide

A solution of isopropanol (225 mL) and small chunks of sodium metal (1.92 g, 83.6 mmol) were heated to reflux for 2.5 hours, until the sodium was consumed. The resulting solution was added while still hot to a solution of 4-fluoro-3-nitro-benzenesulfonamide (8.37 g, 38.0 mmol, example 2, step b) in THF/iPrOH (1/1, v/v, 150 mL) over a 10 minute period and stirred at room temperature for 3.5 hours. The reaction mixture was partitioned between EtOAc and brine and 1 N aqueous HCl. The organic phase was then washed with brine, dried with Na₂SO₄ and evaporated to give the title compound.

Example 2 step d 3-Amino-4-isopropoxy-benzenesulfonamide

Sodium borohydride (1.88 g, 49.6 mmol) was added slowly to a solution of nickel (II) chloride hexahydrate (3.93 g, 16.5 mmol) in methanol (60 mL) at 0° C. and the resulting black suspension was stirred for 30 min at 23° C. The mixture was cooled to 0° C. and 4-isopropoxy-3-nitro-benzenesulfonamide (8.6 g, 33.0 mmol, example 2, step c) was added followed by sodium borohydride (4.38 g, 115.6 mmol). The resulting black suspension was stirred for 30 min at 23° C. Water was added to the reaction mixture to quench excess NaBH₄, followed by addition of saturated aqueous NaHCO₃. The product was extracted with dichloromethane and the organic phase was washed with brine, dried with Na₂SO₄ and evaporated to give the title compound.

Example 2 step e 4-Isopropoxy-3-isothiocyanato-benzenesulfonamide

A solution of sodium bicarbonate (16.8 g, 199.5 mmol) in water (400 mL) was added to 3-amino-4-isopropoxy-benzenesulfonamide (15.3 g, 66.5 mmol, example 2, step d) in a mixture of chloroform (200 mL) and water (200 mL). Thiophosgene (6.37 mL, 83.1 mmol) was then added. The biphasic solution was stirred at room temperature for 1.5 h. The phases were separated and the aqueous phase was extracted with CH₂Cl₂. The organic phase was washed with water, dried (Na₂SO₄), filtered, and concentrated, yielding the crude title compound as a tan solid.

Example 2 step f 4-Isopropoxy-3-thioureido-benzenesulfonamide

Crude 4-isopropoxy-3-isothiocyanato-benzenesulfonamide (17.8 g, 65.2 mmol, example 2, step e) was treated with a 2 M solution of ammonia in MeOH (250 mL) and the resulting solution was stirred at room temperature for 18 h. The reaction mixture was then concentrated to about half the volume until a large amount of tan solid precipitated. The suspension was cooled to 0° C. for 30 minutes and was filtered. The solid was washed with methanol and ether to give the title compound as a cream colored solid.

Example 2 3-(2′,4′-Dimethyl-[4,5′]bithiazolyl-2-ylamino)-4-isopropoxy-benzenesulfonamide.HBr

A mixture of 2-bromo-1-(2,4-dimethyl-thiazol-5-yl)-ethanone.HBr (1.07 g, 3.39 mmol, example 2, step a) and 4-isopropoxy-3-thioureido-benzenesulfonamide (0.98 g, 3.39 mmol, example 2, step f) in ethanol (15 mL) was stirred at room temperature for 2 d. The mixture was filtered, washed with cold EtOH, and air-dried, affording the title compound as a white powder. ¹H NMR (300 MHz, DMSO-d₆) δ 9.67 (s, 1H), 9.00 (d, J=2.26 Hz, 1H), 7.43 (dd, J=2.07, 8.48 Hz, 1H), 7.21 (d, J=8.67 Hz, 1H), 7.14 (br. s, 2H), 7.07 (s, 1H), 4.80 (sept, J=6.03 Hz, 1H), 2.65 (s, 3H), 1.36 (d, J=6.03 Hz, 6H); MS m/e 425.1 (M+H).

Example 3 3-(2′-Amino-4′-methyl-[4,5]bithiazolyl-2-ylamino)-4-methoxy-benzamide.HBr

Example 3 step a 1-(2-Amino-4-methyl-thiazol-5-yl)-2-bromo-ethanone

1-(2-Amino-4-methyl-thiazol-5-yl)-2-bromo-ethanone.HBr was prepared as described in WO 2005/068444. To convert to the corresponding free base, the crude reaction mixture was slowly added to ice-cold sat. aq. NaHCO₃ solution. The precipitate was collected by vacuum filtration and washed with Et₂O. The crude product was recrystallized from EtOH, affording the title compound as an orange powder.

Example 3 step b 4-Methoxy-3-thioureido-benzamide

To a solution of 3-amino-4-methoxybenzamide (2.49 g, 15.0 mmol, Alfa) in acetone (30 mL) at reflux was added benzoyl isothiocyanate (2.22 mL, 16.5 mmol) and the mixture was stirred at reflux for 30 min, then was poured into water. The precipitate was collected by vacuum filtration and was treated with 10% aq. NaOH (15 mL). The mixture was heated to reflux for 40 min, cooled to room temperature, and poured into a mixture of ice and 6 N aq. HCl. The mixture was basified to pH 10 with conc. aq. NH₄OH and the resulting white solid precipitate was collected by vacuum filtration, affording the crude title compound, which was used without further purification.

Example 3 3-(2′-Amino-4′-methyl-[4,5′]bithiazolyl-2-ylamino)-4-methoxy-benzamide.HBr

A mixture of 1-(2-amino-4-methyl-thiazol-5-yl)-2-bromo-ethanone (270 mg, 1.15 mmol, example 3, step a) and 4-methoxy-3-thioureido-benzamide (259 mg, 1.15 mmol, example 3, step b) in ethanol (5 mL) was stirred at room temperature for 18 h. The mixture was filtered, washed with EtOH, and air-dried. The crude product was recrystallized from a mixture of EtOH and water. ¹H NMR (300 MHz, DMSO-d₆) δ ppm 9.82 (s, 1H), 9.25 (br. s, 2H), 8.79 (s, 1H), 7.80 (br. s, 1H), 7.57 (d, J=7.9 Hz, 1H), 7.00-7.17 (m, 3H), 3.92 (s, 3H), 2.45 (s, 3H). MS m/e 362.1 (M+H).

Example 4 (4-Methoxy-pyridin-3-yl)-(6-methyl-6H-imidazo[4′,5′:3,4]benzo[2,1-d]thiazol-2-yl)-amine.TFA

Example 4 step a 3-Isothiocyanato-4-methoxy-pyridine

To a stirred mixture of 3-amino-4-methoxypyridine (2.01 g, 16.2 mmol) and NaHCO₃ (4.08 g, 48.6 mmol) in CHCl₃ and water (1:1, 50 mL) at 4° C. was added thiophosgene (1.5 mL, 19.6 mmol) dropwise. After completion of the addition, the ice bath was removed. The mixture was stirred for 4 hours, the organic layer was separated, and the aqueous layer was extracted with CH₂Cl₂. The combined organic phases were washed with water, dried over Na₂SO₄, filtered, and concentrated to give the title compound as brown solid.

Example 4 step b 1-(4-Methoxy-pyridin-3-yl)-3-(1-methyl-1H-benzoimidazol-4-yl)-thiourea

A mixture of 4-amino-1-methylbenzimidazole (0.100 g, 0.679 mmol) and 3-isothiocyanato-4-methoxy-pyridine (0.113 mg, 0.680 mmol, example 4, step a) in DMF was stirred at room temperature for 64 hours. After removal of DMF in vacuo, the residue was treated with water. The precipitated solid was filtered, washed with water, and dried to give a portion of the title compound. The filtrate was concentrated and the oily brown residue was dried under vacuum to provide a second potion of the title compound.

Example 4 (4-Methoxy-pyridin-3-yl)-(6-methyl-6H-imidazo[4′,5′:3,4]benzo[2,1-d]thiazol-2-yl)-amine.TFA

1-(4-M ethoxy-pyridin-3-yl)-3-(1-methyl-1H-benzoimidazol-4-yl)-thiourea (213 mg, 0.68 mmol, example 4, step b) in acetic acid (1 mL) was treated with 0.50 M Br₂ (1.09 mL, 0.544 mmol) in acetic acid overnight. After evaporation of HOAc in vacuo, CF₃CO₂H was added and then removed in vacuo. The residue was dissolved in a small amount of DMSO and purified by HPLC eluting with water/acetonitrile/0.2% trifluoroacetic acid to provide the title compound as a brown solid. ¹H NMR (400 MHz, MeOH-d₄) δ=10.47 (d, J=1.0 Hz, 1H), 9.41 (s, 1H), 8.50 (dd, J=1.2, 6.6 Hz, 1H), 7.99 (d, J=8.8 Hz, 1H), 7.71 (d, J=8.8 Hz, 1H), 7.66 (d, J=6.6 Hz, 1H), 4.30 (s, 3H), 4.19 (s, 3H); MS m/e 312 (M+H).

Cloning, Expression and Purification

Cloning of human proMMP9

Amino acid numbering for all human proMMP9 constructs was based on UniProtKB/Swiss-Prot P14780, full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1). One construct, proMMP9(20-445) (SEQ ID NO:2), was based on the previously published crystal structure (Elkins, Ho et al. 2002). The construct lacked the signal peptide at the N-terminus and also lacked the four hemopexin-like domains at the C-terminus. An N-terminal truncated construct was also designed with an N-terminus truncation after the first observable electron density in the previously published proMMP9 structure and a single amino acid was removed from the C-terminus to produce proMMP9(29-444) (SEQ ID NO:3). Other truncated constructs were also synthesized without the three fibronectin type-II domains (AFnII), amino acids 216-390. The AFnII constructs were proMMP9(29-444; ΔFnII) (SEQ ID NO:4), proMMP9(67-444; ΔFnII) (SEQ ID NO:5) and proMMP9(20-445; ΔFnII) (SEQ ID NO:6). Binding studies with the proMMP9 proteins without the FnII domains showed that compounds bound with similar affinity compared to the wild-type protein (data not shown).

In order to make the constructs with the FnII domains deleted, proMMP9(29-444; ΔFnII) (SEQ ID NO:4), proMMP9(67-444; ΔFnII) (SEQ ID NO:5) and proMMP9(20-445; ΔFnII) (SEQ ID NO:6), plasmids encoding the different proMMP9 truncations were used as templates for PCR to create two fragments of DNA corresponding to amino acid pairs including: 29-215/391-444, 67-215/391-444, and 20-215/391-445, respectively. Overlapping PCR was used to join the fragments. The 5′ primers had an Nde1 site and a start methionine and the 3′ primers had a stop codon and a Bg12 site. The final PCR products were cloned into the TOPO TA cloning vector (Invitrogen) and the sequences were confirmed. Subsequently the vectors were digested with Nde1 and Bg12 and the sequences were subcloned into Nde1 and BamH1 sites of the T7 expression vector pET11a (Novagen).

Expression of Truncated Forms of Human proMMP9

For expression in E. coli, all of the truncated proMMP9 constructs were transformed into BL21(DE3) RIL cells (Stratagene). Cells were initiated for an overnight culture from glycerol stocks in LB+Ampicillin (100 μg/ml) @ 37° C. shaking at 220 rpms. The overnight culture was subcultured 1:100 in LB+Ampicillin (100 ug/ml) and maintained at 37° C. shaking at 220 rpms. Samples were taken and A600 readings were monitored until an OD of 0.6 was achieved. The culture was induced with 1 mM IPTG and maintained under present growth conditions. Cultures were harvested 3 hours post induction at 6000×g for 10 min. Pellets were washed in 1×PBS with protease inhibitors and stored at −80° C.

Purification of Truncated Forms of Human proMMP9

To purify the truncated proMMP9 proteins from E. coli, cell pellets were suspended in 25 mM Na₂HPO₄ pH 7, 150 mM NaCl, 10 mL/gram cell pellet. The cells were homogenized in a Dounce homogenizer, and then processed twice through a microfluidizer (Microfluidics International Corporation, model M-110Y). The lysate was centrifuged at 32,000×g for 45 minutes at 4° C. The supernatant was discarded. The pellet was suspended in 25 mM Na₂HPO₄ pH 7, 150 mM NaCl, 10 mM DTT, 1 mM EDTA, 10 mL/gram cell pellet. The pellet was homogenized in a Dounce homogenizer, and then centrifuged at 32,000×g for 45 minutes at 4° C. The supernatant was discarded. The pellet was suspended in 7 M urea, 25 mM Tris pH 7.5, 10 mM DTT, 1 mM EDTA, 6.5 mL/gram cell pellet, and then solubilized in a Dounce homogenizer and stirred for approximately 16 hours at ambient temperature. The solubilized protein solution was adjusted to pH 7.5, centrifuged at 45,000×g, 45 minutes at 4° C., and the supernatant, containing the denatured proMMP9, was filtered to 0.8 micron. A 5 mL HiTrap Q Sepharose HP column (GE Healthcare) was prepared according to manufacturer's instructions using Buffer A: 7 M urea, 25 mM Tris pH 7.5 and Buffer B: 7 M urea, 25 mM Tris pH 7.5, 1.0 M NaCl. The protein solution was applied to the HiTrap at 2.5 mL/minute. The column was washed to baseline absorbance with approximately 3.5 CV Buffer A. The proMMP9 was eluted in a 12CV linear gradient from 0% Buffer B to 12% Buffer B. Fractions were collected, analyzed on SDS-PAGE (Novex) and pooled based on purity. The pooled protein was re-natured by drop-wise addition to a solution, stirring and at ambient temperature, of 20 mM Tris pH 7.5, 200 mM NaCl, 5 mM CaCl₂, 1 mM ZnCl₂, 0.7 M L-arginine, 10 mM reduced and 1 mM oxidized glutathione, and was stirred for approximately 16 hours at 4° C. The refolded protein was concentrated to approximately 2.5 mg/mL in Jumbo Sep centrifugal concentrators (Pall) with 10,000 MWCO membranes. The concentrated protein solution was dialyzed at 4° C. for approximately 16 hours against 20 mM Tris pH 7.5, 150 mM NaCl. The dialyzed protein solution was clarified by filtration to 0.8 micron, concentrated to 2 mg/mL as before, centrifuged at 45,000×g for 15 minutes at 4° C. and filtered to 0.2 micron. It was purified on a HiLoad 26/60 Superdex 200 column (GE Healthcare) equilibrated in 20 mM Tris pH 7.5, 200 mM NaCl. Fractions were analyzed by SDS-PAGE and pooled based on purity. The pooled protein was concentrated in a Jumbo Sep concentrator as before and centrifuged at 16,000×g for 10 minutes at 4° C. The protein concentration was determined using Bio-Rad Protein Assay (Bio-Rad Laboratories, Inc.) with bovine serum albumin as a standard. The supernatant was aliquoted, frozen in liquid nitrogen and stored at −80° C.

Full-Length Human proMMP9

Full-length proMMP9(1-707) (SEQ ID NO:1) was expressed in HEK293 cells or in COS-1 cells as a secreted protein using a pcDNA3.1 expression vector. When expressed as a secreted protein in HEK293 cells or COS-1 cells, there is cotranslational removal of the signal peptide, amino acids 1-19 of full-length proMMP9(1-707) (SEQ ID NO:1). The final purified proMMP9(1-707) (SEQ ID NO:1) protein lacks the signal peptide.

Prior to transfection with the proMMP9(1-707) (SEQ ID NO:1) construct, the HEK293 cells were suspension adapted (shake flasks) in a serum free media (Freestyle 293) supplemented with pluronic acid (F-68) at a final concentration of 0.1%. Once cells reached a density of 1.2×10⁶/mL they were transiently transfected using standard methods. Transient transfection of COS-1 cells was done in flasks with adherent cell cultures and serum free media. For both HEK293 and COS-1 cells, the conditioned media was collected for purification of the proMMP9(1-707) (SEQ ID NO:1) protein. 1.0 M HEPES pH 7.5 was added to 9 L of conditioned media for a final concentration of 50 mM. The media was concentrated to 600 mL in a Kvicklab concentrator fitted with a hollow fiber cartridge of 10,000 MWCO (GE Healthcare). This was clarified by centrifugation at 6,000×g, 15 minutes, at 4° C. and then further concentrated to 400 mL in Jumbo Sep centrifugal concentrators (Pall) with 10,000 MWCO membranes. The concentrated protein was dialyzed against 50 mM HEPES pH 7.5, 10 mM CaCl₂, 0.05% Brij 35, overnight at 4° C. and then dialysis was continued for several hours at 4° C. in fresh dialysis buffer. The dialyzed protein was centrifuged at 6,000×g, 15 minutes, at 4° C., and filtered to 0.45 micron. 12 mL of Gelatin Sepharose 4B resin (GE Healthcare) was equilibrated in 50 mM HEPES pH 7.5, 10 mM CaCl₂, 0.05% Brij 35 in a 2.5 cm diameter Econo-Column (Bio-Rad Laboratories). The filtered protein solution was loaded onto the Gelatin Sepharose resin using gravity flow at approximately 3 mL/minute. The resin was washed with 10CV 50 mM HEPES pH 7.5, 10 mM CaCl₂, 0.05% Brij 35 and eluted with 30 mL 50 mM HEPES pH 7.5, 10 mM CaCl₂, 0.05% Brij 35, 10% DMSO, collected in 5 mL fractions. Fractions containing protein, confirmed by A280 absorbance, were dialyzed, in 500 times the volume of the fractions, against 50 mM HEPES pH 7.5, 10 mM CaCl₂, 0.05% Brij 35, overnight at 4° C. Dialysis was continued for an additional 24 hours in two fresh buffer changes. The dialyzed fractions were analyzed on SDS-PAGE and pooled based on purity. The pooled protein was concentrated to 1.2 mg/mL in Jumbo Sep centrifugal concentrators with 10,000 MWCO membranes. Protein concentration was determined with DC™ protein assay (Bio-Rad Laboratories, Inc.). The protein was aliquoted, frozen in liquid nitrogen and stored at −80° C.

Full-Length Rat proMMP9

Amino acid numbering for full-length rat proMMP9 was based on UniProtKB/Swiss-Prot P50282, full-length rat matrix metalloproteinase-9 precursor, proMMP9(1-708) (SEQ ID NO:11). The full-length rat proMMP9 was produced with the same methods as described for full-length human proMMP9. In brief, full-length rat proMMP9(1-708) (SEQ ID NO:11) was expressed in HEK293 cells as a secreted protein using a pcDNA3.1 expression vector. When expressed in HEK293 cells and secreted into the media, there is cotranslational removal of the signal peptide, so the final purified full-length rat proMMP9(1-708) (SEQ ID NO:11) protein lacks the signal peptide.

Human proMMP13

The sequence for proMMP13 was amino acids 1-268 from UniProtKB/Swiss-Prot P45452, proMMP13(1-268) (SEQ ID NO:7). The expression construct included a C-terminal Tev cleavage sequence flanking recombination sequences for use in the Invitrogen Gateway system. The construct was recombined into an entry vector using the Invitrogen Gateway recombination reagents. The resulting construct was transferred into a HEK293 expression vector containing a C-terminal 6×-histidine tag. Protein was expressed via transient transfection utilizing HEK293 cells and secreted into the media. When expressed in HEK293 cells and secreted into the media, there is cotranslational removal of the signal peptide, amino acids 1-19 of proMMP13(1-268) (SEQ ID NO:7). The final purified proMMP13(1-268) (SEQ ID NO:7) protein lacks the signal peptide. HEK293 media were harvested and centrifuged. Media were loaded on GE Healthcare HisTrap FF columns, washed with buffer A (20 mM Tris pH 7.5, 200 mM NaCl, 2 mM CaCl₂, 10 mM imidazole), and eluted with buffer B (20 mM Tris pH 7.5, 200 mM NaCl, 2 mM CaCl₂ 200 mM imidazole). The eluted protein was loaded on a Superdex 200 column equilibrated with buffer C (20 mM HEPES pH 7.4, 100 mM NaCl, 0.5 mM CaCl₂). Fractions containing proMMP13(1-268) (SEQ ID NO:7) were pooled and concentrated to >2 mg/mL.

Human Catalytic MMP3

Catalytic MMP3 was amino acids 100-265 of human MMP3 from UniProtKB/Swiss-Prot P08254, MMP3(100-265) (SEQ ID NO:8). The corresponding nucleotide sequence was subcloned into a pET28b vector to add a C-terminal 6×-Histidine tag and the construct was used for expression in E. coli. The protein was purified to >95% purity from 4.5 M urea solubilized inclusion bodies by standard techniques. Aliquots of purified protein were stored at −70° C. Purified recombinant human catalytic MMP3 is also available from commercial sources (e.g., Calbiochem®, 444217).

Biological Assays ThermoFluor® Assays

Generalized ThermoFluor® methods

The ThermoFluor® (TF) assay is a 384-well plate-based binding assay that measures thermal stability of proteins (Pantoliano, Petrella et al. 2001; Matulis, Kranz et al. 2005). The experiments were carried out using instruments available from Johnson & Johnson Pharmaceutical Research & Development, LLC. TF dye used in all experiments was 1,8-anilinonaphthalene-8-sulfonic acid (1,8-ANS) (Invitrogen: A-47).

Compounds were arranged in a pre-dispensed plate (Greiner Bio-one: 781280), wherein compounds were serially diluted in 100% DMSO across 11 columns within a series. Columns 12 and 24 were used as DMSO reference and contained no compound. For multiple compound concentration-response experiments, the compound aliquots (50 mL) were robotically predispensed directly into black 384-well polypropylene PCR microplates (Abgene: TF-0384/k) using a Cartesian Hummingbird liquid handler (DigiLab, Holliston, Mass.). Following compound dispense, protein and dye solutions were added to achieve the final assay volume of 3 μL. The assay solutions were overlayed with 1 μL of silicone oil (Fluka, type DC 200: 85411) to prevent evaporation.

Assay plates were robotically loaded onto a thermostatically controlled PCR-type thermal block and then heated from 40 to 90° C. at a ramp-rate of 1° C./min for all experiments. Fluorescence was measured by continuous illumination with UV light (Hamamatsu LC6) supplied via fiber optics and filtered through a band-pass filter (380-400 nm; >60D cutoff). Fluorescence emission of the entire 384-well plate was detected by measuring light intensity using a CCD camera (Sensys, Roper Scientific) filtered to detect 500±25 nm, resulting in simultaneous and independent readings of all 384 wells. A single image with 20-sec exposure time was collected at each temperature, and the sum of the pixel intensity in a given area of the assay plate was recorded vs temperature and fit to standard equations to yield the T_(m) (Pantoliano, Petrella et al. 2001).

Thermodynamic parameters necessary for fitting compound binding for each proMMP were estimated by differential scanning calorimetry (DSC) and from ThermoFluor® data. The heat capacity of unfolding for each protein was estimated from the molecular weight and from ThermoFluor® dosing data. Unfolding curves were fit singly, then in groups of 12 ligand concentrations the data were fit to a single K_(D) for each compound.

ThermoFluor® with proMMP9(67-444; ΔFnII) (SEQ ID NO:5)

The protein sample preparations had to include a desalting buffer exchange step via a PD-10 gravity column (GE Healthcare). The desalting buffer exchange was performed prior to diluting the protein to the final assay concentration of 3.5 μM proMMP9(67-444; ΔFnII) (SEQ ID NO:5). The concentration of proMMP9(67-444; ΔFnII) (SEQ ID NO:5) was determined spectrophotometrically based on a calculated extinction coefficient of ε₂₈₀=33900 M⁻¹ cm⁻¹, a calculated molecular weight of 22.6 kDa, and calculated pI of 5.20. ThermoFluor® reference conditions were defined as follows: 80 μg/mL (3.5 μM) proMMP9(67-444; ΔFnII) (SEQ ID NO:5), 50 μM 1,8-ANS, pH 7.0 Buffer (50 mM HEPES pH 7.0, 100 mM NaCl, 0.001% Tween-20, 2.5 mM MgCl₂, 300 μM CaCl₂). The thermodynamic parameters for proMMP9(67-444; ΔFnII) (SEQ ID NO:5) are as follows: T_(m) (° C.)=63 (+/−0.1), Δ_(U)H_((Tm)) (cal mol⁻¹)=105000(+/−5000), Δ_(U)S_((Tm)) (cal mol⁻¹ K⁻¹)=450, Δ_(U)C_(p) (cal mol⁻¹ K⁻¹)=2000.

ThermoFluor® with proMMP9(20-445; ΔFnII) (SEQ ID NO:6)

The protein sample preparations included a desalting buffer exchange step via a PD-10 gravity column (GE Healthcare). The desalting buffer exchange was performed prior to diluting the protein to the final assay concentration of 2.8 μM proMMP9(20-445; ΔFnII) (SEQ ID NO:6). The concentration of proMMP9(20-445; ΔFnII) (SEQ ID NO:6) was determined spectrophotometrically based on a calculated extinction coefficient of ε₂₈₀=39880 M⁻¹ cm⁻¹, a calculated molecular weight of 28.2 kDa, and calculated pI of 5.5. ThermoFluor® reference conditions were define as follows: 80 μg/mL (2.8 μM) proMMP9(20-445; ΔFnII) (SEQ ID NO:6), 50 μM 1,8-ANS, pH 7.0 Buffer (50 mM HEPES pH 7.0, 100 mM NaCl, 0.001% Tween-20, 2.5 mM MgCl₂, 300 μM CaCl₂). The thermodynamic parameters for proMMP9(20-445; ΔFnII) (SEQ ID NO:6) are as follows: T_(m) (° C.)=72 (+/−0.1), Δ_(U)H_((Tm)) (cal mol⁻¹)=160000(+/−5000), Δ_(U)S_((Tm)) (cal mol⁻¹ K⁻¹)=434, Δ_(U)C_(p) (cal mol⁻¹ K⁻¹)=2400.

ThermoFluor® with proMMP13(1-268) (SEQ ID NO:7)

The proMMP13(1-268) (SEQ ID NO:7) protein sample preparations included a desalting buffer exchange step via a PD-10 gravity column (GE Healthcare). The desalting buffer exchange was performed prior to diluting the protein to the final assay concentration of 3.5 μM. The concentration of proMMP13(1-268) (SEQ ID NO:7) was estimated spectrophotometrically based on a calculated extinction coefficient of ε₂₈₀=37000 M⁻¹cm⁻¹, a calculated molecular weight of 30.8 kDa, and calculated pI of 5.33. ThermoFluor® reference conditions were defined as follows: 100 μg/mL proMMP13(1-268) (SEQ ID NO:7), 25 μM 1,8-ANS, pH 7.0 Buffer (50 mM HEPES pH 7.0, 100 mM NaCl, 0.001% Tween-20, 2.5 mM MgCl₂, 300 μM CaCl₂). The thermodynamic parameters for proMMP13(1-268) (SEQ ID NO:7) are as follows: T_(m)(° C.)=67 (+/−0.1), Δ_(U)H_((Tm)) (cal mol⁻¹)=107000(+/−5000), Δ_(U)S_((Tm)) (cal mol⁻¹¹c)=318, Δ_(U)C_(p) (cal mol⁻¹¹c)=2600.

TABLE 1 Representative Thermofluor data for selected compounds proMMP9(20-445; proMMP9(67-444; ΔFnII) ΔFnII) proMMP13(1-268) Exam- (SEQ ID NO: 6) (SEQ ID NO: 5) (SEQ ID NO: 7) ple binding, Kd (μM) binding, Kd (μM) binding, Kd (μM) 1 1.75 0.388 37.48 2 0.10 0.26 0.14 3 0.27 0.56 4.9 4 1.0 0.039 ND

Enzyme Assays

proMMP9/MMP3 P126 Activation Assay

Compounds were assessed for inhibition of proMMP9 activation by catalytic MMP3, MMP3(100-265) (SEQ ID NO:8) using full-length proMMP9(1-707) (SEQ ID NO:1) purified from HEK293 cells and a peptide (Mca-PLGL-Dpa-AR-NH₂, BioMol P-126) that fluoresces upon cleavage by catalytic MMP9. The assay buffer employed was 50 mM Hepes, pH 7.5, 10 mM CaCl₂, 0.05% Brij-35. DMSO was included at a final concentration of 2%, arising from the test compound addition. On the day of assay, proMMP9(1-707) (SEQ ID NO:1) purified from HEK293 cells and MMP3(100-265) (SEQ ID NO:8) were diluted to 400 nM in assay buffer. The reaction volume was 50 μL. In 96-well black plates (Costar 3915), 44 μL of assay buffer was mixed with 1.0 μL of test compound, 2.5 μL of 400 nM proMMP9(1-707) (SEQ ID NO:1) purified from HEK293 cells and the reaction was initiated with 2.5 μL of 400 nM MMP3(100-265) (SEQ ID NO:8). The plate was sealed and incubated for 80 min at 37° C. Final concentrations were 20 nM proMMP9(1-707) (SEQ ID NO:1) purified from HEK293 cells and 20 nM MMP3(100-265) (SEQ ID NO:8), and concentrations of test compounds were varied to fully bracket the IC₅₀. Immediately following the 80 min incubation, 50 μL of 40 μM P-126 substrate was added (freshly diluted in assay buffer), and the resulting activity associated with catalytic MMP9 was kinetically monitored at 328 nm excitation, 393 nm emission for 10-15 min at 37° C., using a Spectramax Gemini XPS reader (Molecular Devices). Reactivity of residual MMP3 towards P-126 substrate was minimal under these conditions. Initial velocities were plotted by use of a four-parameter logistics equation (GraphPad Prism® software) for determination of IC₅₀.

ProMMP13/Plasmin P126 Activation Assay

Compounds were assessed for inhibition of proMMP13 activation by plasmin using a peptide (Mca-PLGL-Dpa-AR-NH₂, BioMol P-126) that fluoresces upon cleavage by catalytic MMP13. The assay buffer employed was 50 mM Hepes, pH 7.5, 10 mM CaCl₂, 0.05% Brij-35. DMSO was included at a final concentration of 2%, arising from the test compound addition. On the day of assay, proMMP13(1-268) (SEQ ID NO:7) purified from HEK293 cells and plasmin were diluted to 160 nM and 320 nM, respectively, in assay buffer. The reaction volume was 50 μL. In 96-well black plates (Costar 3915), 44 μL of assay buffer was mixed with 1.0 μL of test compound, 2.5 μL of 160 nM proMMP13(1-268) (SEQ ID NO:7), and the reaction was initiated with 2.5 μL of 320 nM plasmin. The plate was sealed and incubated for 40 min at 37° C. Final concentrations were 8 nM proMMP13(1-268) (SEQ ID NO:7) and 16 nM plasmin, and concentrations of test compounds were varied to fully bracket the IC₅₀. Immediately following the 40 min incubation, 50 μL of 40 μM P-126 substrate was added (freshly diluted in assay buffer), and the resulting activity associated with catalytic MMP13 was kinetically monitored at 328 nm excitation, 393 nm emission for 10-15 min at 37° C., using a Spectramax Gemini XPS reader (Molecular Devices). Plasmin was not reactive towards P-126 substrate under these conditions. Initial velocities were plotted by use of a four-parameter logistics equation (GraphPad Prism® software) for determination of IC₅₀.

ProMMP9/MMP3 DQ Gelatin Activation Assay

Compounds were assessed for inhibition of proMMP9 activation by catalytic MMP3 using a quenched fluorescein gelatin substrate (DQ gelatin, Invitrogen D12054) that fluoresces upon cleavage by activated MMP9. The assay buffer employed was 50 mM Hepes, pH 7.5, 10 mM CaCl₂, 0.05% Brij-35. DMSO was included at a final concentration of 0.2%, arising from the test compound addition. On the day of assay, full-length proMMP9(1-707) (SEQ ID NO:1) from COS-1 cells and catalytic MMP3(100-265) (SEQ ID NO:8) were diluted to 60 nM and 30 nM, respectively, in assay buffer. Test compounds in DMSO were diluted 250-fold in assay buffer at 4× the final concentration. The reaction volume was 12 μL, and all reactions were conducted in triplicate. In 384-well half-volume plates (Perkin Elmer ProxiPlate 384 F Plus, 6008260), 4 μL of test compound in assay buffer was mixed with 4 μL of 60 nM full-length proMMP9(1-707) (SEQ ID NO:1) from COS-1 cells. The plate was sealed and incubated for 30 min at 37° C. Final concentrations were 20 nM full-length proMMP9(1-707) (SEQ ID NO:1) from COS-1 cells and 10 nM MMP3(100-265) (SEQ ID NO:8), and concentrations of test compounds were varied to fully bracket the IC₅₀. Immediately following the 30 min incubation, 4 μL of 40 μg/ml DQ gelatin substrate was added (freshly diluted in assay buffer), and incubated for 10 min at room temperature. The reaction was stopped by the addition of 4 μL of 50 mM EDTA, and the resulting activity associated with catalytic MMP9 was determined at 485 nm excitation, 535 nm emission using an Envision fluorescent reader (Perkin Elmer). Reactivity of residual MMP3 towards DQ gelatin was minimal under these conditions. Percent inhibition of test compounds were determined from suitable positive (DMSO only in assay buffer) and negative (EDTA added prior to reaction initiation) controls. Plots of % inhibition vs. test compound concentration were fit to a four-parameter logistics equation (GraphPad Prism® software) for determination of IC₅₀.

Catalytic Enzyme Assays

Selected compounds that were active in the proMMP9 activation assays were subsequently tested in catalytic MMP3 and catalytic MMP9 assays. Compounds that inhibited catalytic MMP3 or catalytic MMP9 were considered false positives in the proMMP9 activation assay.

Catalytic MMP3

Compounds were assessed for inhibition of human catalytic MMP3, MMP3(100-265) (SEQ ID NO:8), using a peptide (Mca-RPKPVE-Nva-WRK(Dnp)-NH₂, Bachem M2110) that fluoresces upon cleavage by catalytic MMP3. The assay buffer employed was 50 mM Hepes, pH 7.5, 10 mM CaCl₂, 0.05% Brij-35. DMSO was included at a final concentration of 2%, arising from the test compound addition. The reaction volume was 100 μL. In 96-well black plates (Costar 3915), 44 μL of assay buffer was mixed with 1.0 μL of test compound, and 5 μL of 400 nM human catalytic MMP3 and the mixture was preincubated at 37° C. for 10 minutes. The reaction was initiated with 50 μL of 40 μM M-2110 substrate (freshly diluted in assay buffer), and the resulting activity associated with catalytic MMP3 was kinetically monitored at 328 nm excitation, 393 nm emission for 5-15 min at 37° C., using a Spectramax Gemini XPS reader (Molecular Devices). Initial velocities were plotted by use of a four-parameter logistics equation (GraphPad Prism® software) for determination of IC50, if required. Final concentrations employed were 20 nM catalytic MMP3 and 20 μM M2110 substrate.

Catalytic MMP9

Compounds were assessed for inhibition of human catalytic MMP9 (BioMol SE-244), using a peptide (Mca-PLGL-Dpa-AR-NH₂, BioMol P-126) that fluoresces upon cleavage by catalytic MMP9. The assay buffer employed was 50 mM Hepes, pH 7.5, 10 mM CaCl₂, 0.05% Brij-35. DMSO was included at a final concentration of 2%, arising from the test compound addition. The reaction volume was 100 μL. In 96-well black plates (Costar 3915), 44 μL of assay buffer was mixed with 1.0 μL of test compound, and 5 μL of 100 nM human catalytic MMP9 and the mixture was preincubated at 37° C. for 10 minutes. The reaction was initiated with 50 μL of 40 μM P-126 substrate (freshly diluted in assay buffer), and the resulting activity associated with catalytic MMP9 was kinetically monitored at 328 nm excitation, 393 nm emission for 5-15 min at 37° C., using a Spectramax Gemini XPS reader (Molecular Devices). Initial velocities were plotted by use of a four-parameter logistics equation (GraphPad Prism® software) for determination of IC50, if required. Final concentrations employed were 5 nM catalytic MMP9 and 20 μM P-126 substrate.

TABLE 2 Representative enzyme assay data for selected compounds proMMP9/MMP3 ProMMP9/MMP3 ProMMP13/Plasmin P126 DQ gel P126 Exam- Activation Assay, Activation Assay, Activation Assay, ple IC₅₀ (μM) IC₅₀ (μM) IC₅₀ (μM) 1 1.3 1.5 ND 2 0.18 ND 3.3 3 0.85 ND ND 4 0.11 ND ND Catalytic MMP9 Catalytic MMP3 Example IC50 (μM) IC50 (μM) 1 ~40 >50

Cell-Based Assays

Activation of proMMP9 in Rat Synoviocyte Cultures

A primary synoviocytes line was derived from the periarticular tissue of arthritic rats. Arthritis was induced in female Lewis rats following an i.p. administration of streptococcal cell wall peptidoglycan polysaccharides (Cromartie, Craddock et al. 1977). Rats with established arthritis were sacrificed, and hind-limbs were severed, immersed briefly in 70% ethanol, and placed in a sterile hood. The skin was removed and the inflamed tissue surrounding the tibia-tarsal joint was harvested using a scalpel. Tissue from six rats was pooled, minced to approximately 8 mm³ pieces, and cultured in Dulbecco's Modified Eagle's Medium (DMEM) containing 15% fetal calf serum (FCS). In the following weeks, cells migrated out of the tissue piece, proliferated, and formed a monolayer of adherent cells. The synoviocytes were lifted from culture plates with 0.05% trypsin and passaged weekly at 1:4 ratios in DMEM containing 10% FCS. Synoviocytes were used at passage 9 to investigate the ability of Example 2 to inhibit the maturation of MMP9 to active form.

Rat synoviocytes spontaneously expressed and activated MMP9 when cultured in collagen gels and stimulated with tumor necrosis factor-alpha (TNFα) (FIG. 1 and Table 3). Eight volumes of an ice-cold solution of 3.8 mg/mL rat tail collagen (Sigma Cat #C3867-1VL) were mixed with 1 volume of 1 M sodium bicarbonate and 1 volume of 10× Roswell Park Memorial Institute medium. The pH of the mixture was adjusted to pH 7 with 1 N sodium hydroxide and equal volumes of the pH-adjusted collagen solution were mixed with DMEM containing 0.8 million synoviocytes per mL. One half mL volumes were dispensed into Costar 24-well culture dishes and placed for one hr at 37° C. and 5% CO₂, during which time the collagen solution formed a gel. Individual gels were dislodged into wells of 12-well Costar plates containing 1 mL/well of DMEM adjusted to contain 0.05% BSA and 100 ng/mL mouse TNFα (R&D Systems Cat #410-MT-010). The plates were agitated 10 seconds to ensure that the collagen gels did not adhere to the well bottoms. After overnight culture at 37° C. and 5% CO₂, wells were adjusted to contain an additional 0.5 mL of DMEM containing 0.05% BSA and Example 2 at 4× the final desired concentration (final culture volumes were 2 mL). The plates were cultured an additional 48 hrs, at which time 1 mL of conditioned media were harvested into fresh eppendorf tubes containing 40 μL/mL of a 50% slurry of gelatin-conjugated sepharose (GE Healthcare Cat #17-0956-01). Samples were rotated for 2 hrs at 4° C. before centrifugation 1 min×200 g. Supernatants were discarded. The gelatin-sepharose pellets were washed once with 1 mL of ice cold DMEM, resuspended in 50 μL of 2× reducing Leamli buffer and heated 5 min at 95° C. Fifteen μL of eluted proteins were resolved on 4-12% NuPAGE gels and transferred to 0.45 μm pore-sized nitrocellose blots. Next, blots were incubated in blocking buffer (5% milk in Tris-buffered saline containing 0.1% Tween-20) for 1 hr at RT and probed overnight (4° C.) with blocking buffer containing 1 μg/mL primary antibodies. Blots were next probed 1 hr at RT with 1/10,000 dilutions of goat anti-mouse IgG-HRP or goat anti-rabbit IgG-HRP (Santa Cruz) in blocking buffer and developed using SuperSignal® West Fempto Maximum Sensitivity Substrate. Chemiluminesence signal was analyzed using a ChemiDoc imaging system (BioRad Laboratories) and Quantity One® image software. Electrophoretic mobility was estimated based on the mobility of standards (Novex Sharp Pre-Stained Protein Standards P/N 57318).

Mouse mAb-L51/82 (UC Davis/NIH NeuroMab Facility, Antibody Incorporated) was used to detect pro and processed forms of MMP9. Synoviocyte-conditioned media contained an approximately 80 kD form of MMP9 (FIG. 1A, lane 2). In the presence of 0.37-10 μM Example 2 (FIG. 1A, lanes 3-6), the 80 kD active MMP9 form was reduced in a dose dependent fashion, and a form of approximately 86 kD appeared. The 86 kD form was predominant in the presence of 10 μM Example 2 (FIG. 1A, lane 6). Lane 1 was loaded with a standard containing 3 ng of full-length rat proMMP9(1-708) (SEQ ID NO:11) and 3 ng of full-length rat proMMP9(1-708) (SEQ ID NO:11) converted to catalytic rat MMP9 by catalytic MMP3. The electrophoretic mobility of the 80 kD form present in synoviocyte conditioned medium was the same as the active MMP9 standard. The 86 kD form produced by synoviocytes in the presence of Example 2 demonstrated greater mobility than the full-length rat proMMP9(1-708) (SEQ ID NO:11) standard which ran with a mobility of approximately 100 kD. The 86 kD form demonstrated a mobility similar to an incompletely processed intermediate form described previously that retains the cysteine switch and lacks catalytic activity (Ogata, Enghild et al. 1992).

ProMMP9 is activated when cleaved between R106 and F107 (Ogata, Enghild et al. 1992). A rabbit polyclonal antibody (pAb-1246) was generated to the active MMP9 N-terminal neoepitope using an approach similar to that reported previously (Duncan, Richardson et al. 1998). Rabbits were immunized and boosted with a peptide, human MMP9(107-113) (SEQ ID NO:9) conjugated to keyhole limpet hemocyanin, and antibodies were affinity purified from serum using FQTFEGD-conjugated agarose affinity resin and 100 mM glycine (pH 2.5) elution. To resolve N-terminal neoepitope antibodies from antibodies directed to other epitopes within the sequence, eluted antibody was dialyzed in PBS and cross-absorbed by mixing with a peptide, human proMMP9(99-113) (SEQ ID NO:10), that was conjugated to agarose. The unbound fraction containing N-terminal neoepitope antibodies was recovered and was designated pAb-1246.

FIG. 1B, lane 1 demonstrated that pAb-1246 bound the 80 kD active MMP9 standard, but did not recognize the 100 kD proMMP9 standard. pAb-1246 detected 80 kD active MMP9 in synoviocyte conditioned medium, and Example 2 caused a dose-dependent reduction in active MMP9 (FIG. 1B, lanes 2-6). Band chemiluminescence intensities were measured directly and reported in Table 3. The production of active MMP9 was inhibited by Example 2 with an IC₅₀ of approximately 1.1 μM. pAb-1246 did not recognize the 86 kD form, providing further evidence that this likely represented an intermediate form whose further maturation was blocked by Example 2.

TABLE 3 Example 2 blocked production of active MMP9 by rat synoviocytes ^(a) Signal of 80 kD band Example 2, μM (INT*mm²) ^(b) % Inhibition ^(c) 0 84384 0 0.37 μM  74381 12 1.1 μM 45381 46 3.3 μM 11554 86  10 μM 2578 97 ^(a) Rat synoviocytes embedded in collagen gels were stimulated 72 hrs with TNFα. Cultures were supplemented with the indicated concentrations of Example 2 for the final 48 hrs and conditioned media were assessed for the 80 kD active form of MMP9 by Western blotting with pAb-1246 developed against the N-terminal activation neoepitope. ^(b) Chemiluminesence captured during a 30 s exposure was analyzed using a ChemiDoc imaging system (BioRad Laboratories) and Quantity One ® image software. Signals were measured within uniform sized boxes drawn to circumscribe the 80 kD bands and were the product of the average intensity (INT) and the box area (mm²). Values given have been corrected for background signal. ^(c) Percent signal reduction relative to the signal generated by synoviocytes cultured in the absence of Example 2. Activation of proMMP9 by Human Fetal Lung Fibroblast Cultures

Example 2 was assessed additionally for ability to block the maturation of proMMP9 to active MMP9 in cultures of human fetal lung fibroblasts (HFL-1, American Type Culture Collection #CCL-153). Unlike rat synoviocytes, HFL-1 cells were unable to process proMMP9 to the active form without addition of neutrophil elastase. Elastase did not directly cause processing of recombinant proMMP9 (data not shown). Rather, the function of elastase in this assay may be to inactivate tissue inhibitors of matrix metalloproteinases (TIMPs) that repress endogenous pathways of MMP9 activation (Skold, Liu et al. 1999).

HLF-1 were maintained in monolayer culture in DMEM with 10% FCS and were used between passage numbers 5-15. HLF-1 were embedded in collagen gels as described for rat SCW synoviocytes (vida supra). Half mL gels containing 0.4 million cells were dislodged into wells of 12 well Costar plates containing 1 mL/well of DMEM adjusted to contain 0.05% BSA and 100 ng/mL human TNFα (R&D Systems Cat #210-TA/CF). After overnight culture (37° C. and 5% CO₂) wells were adjusted to contain an additional 0.5 mL of DMEM containing 0.05% BSA and with or without 13.2 μM Example 2 (final concentration was 3.3 μM Example 2). Next, cultures were adjusted to contain 30 nM human elastase (Innovative Research). The plates were cultured an additional 72 hrs, at which time MMP9 secreted into the conditioned media was bound to gelatin-sepharose and evaluated by Western blot analysis as described for the rat synoviocyte cultures (vida supra). mAb-51/82 detected three forms of MMP9 in HFL-1 cultures.

These included a form of approximately 100 kD with mobility similar to recombinant rat proMMP9, an approximately 80 kD form with mobility similar to rat active MMP9, and an approximately 86 kD intermediate form. The band intensities are provided in Table 4. In the absence of Example 2, most of the MMP9 was present as the 80 kD form. In the presence of Example 2, the 80 kD form was a minor fraction of the total signal while nearly half of the signal were contributed each by the 100 kD and 86 kD forms. The total signal of the three bands was similar with or without Example 2. These data indicate that the 100 kD and 86 kD forms of MMP9 were effectively stabilized by Example 2 and the formation of the 80 kD form was suppressed.

TABLE 4 Example 2 blocked processing of MMP9 by HFL-1 cells^(a) Ex- am- ple 2, 3.3 Signal (INT * mm²)^(b) Percent of total signal μM 100 kD 86 kD 80 kD Total 100 kD 86 kD 80 kD − 17190 24858 61925 103973 16 24 60 + 42107 43147 6092 91346 46 47 7 ^(a)Human fetal lung fibroblasts (HFL-1) embedded in collagen gels were stimulated 90 hrs with TNFα. Cultures were supplemented with or without 3.3 μM Example 2 and with 30 nM elastase for the final 72 hrs and conditioned media were assessed for the MMP9 forms by Western blotting with mAb-L51/82. ^(b)Chemiluminesence captured during a 150 s exposure was analyzed using a ChemiDoc imaging system (BioRad Laboratories) and Quantity One ® image software. Signals were measured within uniform sized boxes drawn to circumscribe the bands and were the product of the average intensity (INT) and the box area (mm²). Values given have been corrected for background signal.

A second experiment was performed to determine if the 80 kD form was mature active MMP9 and to determine the potency of Example 2 as an inhibitor of MMP9 maturation in this assay. HFL-1 cells embedded in collagen gels were cultured as described above in the presence of TNFα overnight and the cultures were then adjusted to contain 30 nM elastase and graded concentrations of Example 2 for an additional 72 hrs at which time MMP9 secreted into the conditioned media was bound to gelatin-sepharose and evaluated by Western blot analysis for active MMP9 using pAb-1246 raised against the N-terminal neoepitope of active MMP9 (Table 5). In the absence of Example 2, pAb-1246 readily detected MMP9 with an electrophoretic mobility of approximately 80 kD. Example 2 effectively inhibited the ability of HFL-1 cultures to process proMMP9 to active MMP9. Inhibition occurred over a dose range with an IC₅₀ of approximately 0.3 μM Example 2.

TABLE 5 Example 2 blocked production of active MMP9 by human fetal lung fibroblasts ^(a) Signal of 80 kD band Example 2, μM (INT*mm²) ^(b) % Inhibition ^(c) 0 168781 0 0.12 μM  168211 0 0.37 μM  45996 73 1.1 μM 1747 99 3.3 μM 152 100  10 μM 0 100 ^(a) Human fetal lung fibroblasts (HFL-1) embedded in collagen gels were stimulated 90 hrs with TNFα. Cultures were supplemented with the indicated concentrations of Example 2 and 30 nM elastase for the final 72 hrs and conditioned media were assessed for active MMP9 by Western blotting with pAb-1246 developed against the N-terminal activation neoepitope. ^(b) Chemiluminesence captured during a 10 s exposure was analyzed using a ChemiDoc imaging system (BioRad Laboratories) and Quantity One ® image software. Signals were measured within uniform sized boxes drawn to circumscribe the 80 kD bands and were the product of the average intensity (INT) and the box area (mm²). Values given have been corrected for background signal. ^(c) Percent signal reduction relative to the signal generated by HFL-1 cells cultured in the absence of Example 2.

In Vivo Studies

Expression and Activation of proMMP9 In Vivo is Associated with Rat SCW-Arthritis

MMP9 protein expression was reportedly increased in the synovial fluid of patients with rheumatoid arthritis (Gruber, Sorbi et al. 1996). A preliminary study was performed to assess MMP9 expression and activation in a rat model of arthritis.

A polyarthritis can be induced in female Lewis rats following i.p. administration of streptococcal cell wall (SCW) proteoglycan-polysaccharides (PG-PS) (Cromartie, Craddock et al. 1977). The model has an acute phase (days 3-7) that is complement and neutrophil-dependent and that resolves. A chronic erosive phase begins at about day ten and is dependent on the development of specific T cell immunity to the PG-GS, which resists digestion and remains present in synovial macrophages for months. Like rheumatoid arthritis, SCW-induced arthritis is reduced by TNF inhibitors, and the dependence of SCW-induced arthritis on macrophages (Richards, Williams et al. 2001) and the strong association of rheumatoid arthritis severity with synovial-tissue macrophage counts (Haringman, Gerlag et al. 2005) makes SCW-arthritis an attractive model for testing potential therapeutic agents.

SCW PG-PS 10S (Beckton Dickinson Cat #210866) suspended in saline was vortexed for 30 seconds and sonicated for 3 min with a probe type sonicator prior to injection. Female Lewis (LEW/N) rats, 5-6 weeks of age (80-100 g) were injected (i.p.) with SCW PG-PS (15 μg of rhamnose/gram BW) in the lower left quadrant of the abdomen using a 1 mL syringe fitted with a 23-gauge needle. Control (disease-free) rats were treated in a similar manner with sterile saline. Control rats were sacrificed on day 5 and groups of SCW-injected rats were sacrificed on day 5 when acute inflammation was maximal or on day 18 when chronic inflammation was established.

Hind-limbs were skinned, severed just above the tibia-tarsus joint and below the metatarsals, and the tibia-tarsus joints (ankles) were weighed, snap frozen and pulverized on dry ice using a hammer and anvil. The pulverized tissue was suspended in 3 volumes (w:v) of ice-cold homogenization buffer containing 50 mM Tris pH 7.5, 150 mM NaCl, 5 mM EDTA, 1% Triton X100, 0.05% Brij 30, 10% dimethylsulfoxide and Complete EDTA-free Protease Inhibitor Cocktail (Roche Diagnostics). The suspended tissue was homogenized sequentially with a Kinematica AG Polytron and a Dounce homogenizer. Homogenates were centrifuged at 16,000×g for 10 min at 4° C. and the soluble fractions were saved. Dimethylsulfoxide was removed from a portion of each soluble fraction using PD MiniTrap™ G-25 desalting columns (GE Healthcare). Homogenates (0.25 mL), free of DMSO, were diluted with an equal volume of binding buffer (i.e., homogenization buffer without dimethylsufoxide) and adjusted to contain 50 μL of a 50% slurry of gelatin-conjugated sepharose. Following 2 hours of rotation at 4° C. the beads were washed twice in binding buffer and eluted in 100 μL 2×-reducing Laemmli buffer with heating to 95° C. for 5 minutes. Eluates (20 μL) were resolved on 4-12% NuPAGE gels, transferred to 0.45 μm pore-sized nitrocellose and immunoblotted for detection of proMMP9, active MMP9, and other processed forms using mAb-L51/82 and pAb-1246 as described above for detection of MMP9 forms in synoviocyte and HFL-1 cell conditioned media.

In healthy ankles of rats administered saline, mAb-L51/82 detected small amounts of an approximately 100 kD (proMMP9) and an approximately 80 kD form of MMP9 (FIG. 2A, lanes 1 and 2). proMMP9 was increased markedly in ankle homogenates 5 and 18 days after SCW-administration (FIG. 2A, lanes 3-5 and 6-8, respectively). The 80 kD MMP9 was increased mildly 5 days after SCW-administration (FIG. 2A, lanes 3-5) and was increased markedly 18 days after SCW-administration (FIG. 2A, lanes 6-8). In healthy ankles of rats administered saline, mAb-1246 detected small amounts active MMP9 at 80 kD (FIG. 2B, lanes 1 and 2). The 80 kD active MMP9 was increased mildly 5 days after SCW-administration (FIG. 2A, lanes 3-5) and was increased markedly 18 days after SCW-administration (FIG. 2A, lanes 6-8).

Efficacy of Example 2 in Rats with SCW Arthritis

Having shown that active MMP9 is increased in rats with SCW-induced arthritis, we next sought to determine the ability of Example 2 to reduce disease severity and to reduce active MMP9.

Example 2 Reduced Ankle Swelling of Rats with SCW-Induced Arthritis.

To induce arthritis, Female Lewis (LEW/N) rats, 5-6 weeks of age (80-100 g) were injected (i.p.) with SCW PG-PS as described above. Eighteen days later, arthritis was well established. Calipers were used to measure the width (anterior to posterior surface) of the left and right hind ankles of each rat. Each ankle was measured 3 times and averaged, and treatment groups were randomized based on ankle thickness (Table 6). Commencing on day 18, randomized groups of arthritic rats (n=5 rats/group) received vehicle or 5, 20, or 50 mg/kg Example 2 BID by oral gavage. Vehicle consisted of an aqueous mixture containing 2% (v:v) N-methylpyrrolidone, 5% (v:v) glycerine, and 20% (w:v) captisol. Treatment continued daily through the morning of day 26.

By day 18 mean ankle thickness was increased an average of >4.4 mm compared to disease free rats. Rats treated with vehicle alone continued to gradually develop a more severe arthritis based on ankle thickness measurements over the eight-day treatment period (Table 6). Treatment with Example 2 induced a dose-dependent decrease in ankle thickness measurements. By day 26, the disease associated increase in ankle thickness had been reduced 27, 37, and 46 percent by 5, 20, and 50 mg/kg Example 2, respectively.

TABLE 6 Ankle thickness of rats with SCW-arthritis dosed with vehicle vs. Example 2 Ankle thickness Day 26 (mm)^(a) Δ mm % Treatment Day 18 Day 26 (vs. group 1) Inh Group 1: mean (n = 4) 7.20 7.26 0 100 Sterile Saline SD 0.043 0.012 Vehicle p-value^(b) 0.0000 0.0001 Day 18-26 Group 2: mean (n = 5) 11.86 12.31 5.04 0 PG-PS SD 0.77 1.26 (15 μg/gramBW) Vehicle p-value* na na Day 18-26 Group 3: mean (n = 5) 11.79 10.93 3.67 27 PG-PS SD 0.56 0.21 (15 μg/gramBW) Example 2 p value* 0.88 0.043 (5 mg/kg) Day 18-26 Group 4: mean (n = 5) 11.76 10.42 3.15 37 PG-PS SD 0.73 0.93 (15 μg/gramBW) Example 2 p-value* 0.85 0.028 (20 mg/kg) Day 18-26 Group 5: mean (n = 5) 11.68 9.99 2.73 46 PG-PS SD 0.62 0.73 (15 μg/gramBW) Example 2 p-value* 0.71 0.0075 (50 mg/kg) Day 18-26 ^(a)Calipers were used to measure the width (anterior to posterior surface) of the left and right hind ankles of each rat. Each ankle was measured 3 times and averaged. ^(b)Student's t-test vs. group 2

Hind paw inflammation clinical scores were assigned based on swelling and erythema. By day 18, nearly all rats induced with SCW PG-PS had a clinical score of 8 based on an 8-point scale (Table 7). Treatment with Example 2 induced a dose dependent decrease in clinical score measurements with significant effects emerging at the 20 mg/kg dose (Table 7).

TABLE 7 Clinical Scores of rats with SCW-arthritis dosed with vehicle vs. Example 2 Clinical Scores (0-8) ^(a) Δ Day 18 Treatment Day 18 Day 26 vs. day 26 Group 1: mean (n = 4) 0 0 0 Sterile Saline SD 0 0 Vehicle p-value ^(b) <0.0001 Day 18-26 Group 2: mean (n = 5) 7.80 7.80 0 PG-PS (15 μg/gramBW) SD 0.45 0.45 Vehicle p-value na Day 18-26 Group 3: mean (n = 5) 8.00 6.80 −1.20 PG-PS (15 μg/gramBW) SD 0.00 1.09 Example 2 (5 mg/kg) p-value 0.095 Day 18-26 Group 4: mean (n = 5) 8.00 5.20 −2.80 PG-PS (15 μg/gramBW) SD 0.00 1.79 Example 2 (20 mg/kg) p-value 0.014 Day 18-26 Group 5: mean (n = 5) 7.80 4.40 −3.40 PG-PS (15 μg/gramBW) SD 0.45 1.67 Example 2 (50 mg/kg) p-value 0.0023 Day 18-26 ^(a) Hind paw inflammation clinical scores were assigned based on swelling and erythema as follows: 1 = ankle involvement only; 2 = involvement of ankle and proximal ½ of tarsal joint; 3 = involvement of the ankle and entire tarsal joint down to the metatarsal joints; and 4 = involvement of the entire paw including the digits. Scores of both hind-paws were summed for a maximal score of 8. ^(b) Student's t-test vs. group 2 Example 2 Reduced Active MMP9 in Ankles of Rats with SCW-Induced Arthritis Demonstrated by Western Blot Analysis

Rats in the study reported in Tables 6 and 7 were sacrificed on day 26 four hours after the AM dose Ankles harvested from the right-hind-limbs were processed by the method described above. Pro and active MMP9 were abundantly present in ankles of SCW-induced vehicle-treated rats (FIGS. 3A and 3B, lanes 1-3). Treatment of rats with Example 2 did not reduce the abundance of proMMP9 (FIG. 3A, lanes 4-9). However, treatment of rats with Example 2 resulted in a notable reduction in the active 80 kD form of MMP9 detected with pAb-1246 (FIG. 3B, lanes 4-9 vs. 1-3) and with mAb-L51/82 (FIG. 3A, lanes 4-9 vs. 1-3).

Example 2 Reduced MMP9 Mediated Gelatinase Activity in the Livers of Rats with SCW Arthritis

In situ zymography provides an alternative approach to assess active MMP9 in tissues (Frederiks and Mook 2004). Tissue sections are overlain with fluorescein-conjugated gelatin wherein the conjugation is sufficiently dense to cause the fluorescein to be dye-quenched (DQ). Proteolytic degradation of the DQ-gelatin releases the fluorescein from the quenching effect giving rise to bright green fluorescence at the site of degradation. Because in situ zymography requires the use of frozen sections, calcified tissues are problematic. However, an additional feature of the SCW arthritis model is the development of hepatic granulomatous disease (Wahl, Allen et al. 1986), and MMP9 reportedly plays a role in macrophage recruitment in the granulomas response to mycobacteria (Taylor, Hattie et al. 2006). Consequently, granulomatous livers from SCW-treated rats were assessed for active MMP9 by in situ zymography.

As described above, Female Lewis (LEW/N) rats, 5-6 weeks of age (80-100 g) were injected (i.p.) with saline or SCW PG-PS. On day 28, when the granulomatous response was well established, animals were sacrificed and livers were frozen in OCT cryo-sectioning medium and 10 μm sections were cut on a Cryome HM 500 M cryotome and mounted on glass microscope slides. Sections were air dried briefly. MMP9 was confirmed as the source of the gelatinase activity in the liver by treating liver sections with monoclonal antibodies directed against the active site of the two major gelatinases MMP9 and MMP2. Liver sections overlain with 50 μL of 100 μg/mL neutralizing mouse monoclonal antibodies directed against MMP9 (Calbiochem, clone 6-6B), or MMP2 (Millipore, clone CA-4001), or with PBS for 1 hr at room temperature. Tissues were rinsed once with PBS, blotted, and briefly air dried and then overlain with DQ-gelatin (Invitrogen) dissolved to 1 mg/mL in deionized water and then diluted 1:10 in 1% wt/vol low gelling point agarose type VII (Sigma) in PBS. The sections were covered with coverslips, incubated in the dark at room temperature for 20 min, and imaged on an Olympus IX80 inverted microscope fitted with fluorescence optics, using SlideBook™ imaging software (Intelligent Imaging Innovations, Inc., Philadelphia, Pa.; version 5.0). Fluorescence intensity was determined (Table 8). When compared to a saline-treated rat, gelatinase activity was abundantly expressed in granulomatous liver sections obtained from a rat with SCW arthritis. The activity in the granulomatous liver sections was almost completely inhibited by treatment with anti-MMP9 monoclonal antibody but not by treatment with anti-MMP2 monoclonal antibody.

TABLE 8 Indentification of MMP9 as the gelatinase responsible for signals detected by in situ zymography in SCW-granulomatous livers Disease Intensity (RLU × 10⁶) induction Section treatment Mean SD Saline-healthy PBS 11.4 2.91 SCW- PBS 109 19.3 granulomatous Anti-MMP9 1.02 0.17 Anti-MMP2 128 36.2 Key: RLU = relative light units; SCW = Streptococcal cell wall peptidoglycan-polysaccharide equivalent to 15 μg rhamnose/gram BW.

Next, liver in situ zymography was used to assess the relative presence of active MMP9 in rats dosed with vehicle vs. Example 2. Female Lewis (LEW/N) rats, 5-6 weeks of age (80-100 g) were injected (i.p.) with saline or SCW PG-PS. Commencing on day 25, randomized groups of rats (n=3 rats/group) received vehicle or 20 or 50 mg/kg Example 2 BID by oral gavage. Vehicle consisted of an aqueous mixture containing 2% (v:v) N-methylpyrrolidone, 5% (v:v) glycerine, and 20% (w:v) captisol. Treatment continued daily through the morning of day 28. Four hrs after the AM dose on day 28, rats were sacrificed and livers assessed for active MMP9 by in situ zymography (Table 9). Gelatinase activity was increased markedly in SCW-induced rats, but activity was reduced by approximately 80% in animals treated with 50 mg/kg Example 2.

TABLE 9 In situ zymography determination of gelatinase activity in livers of SCW-induced rats dosed with vehicle vs. Example 2 t-test vs. Intensity (RLU × 10⁶) SCW- Treatment Rat 1 Rat 2 Rat 3 Mean SD vehicle Saline 3.3 1.1 1.6 2.0 1.15 0.001 Vehicle Day 25-28 SCW 65.1 43.4 58.9 55.8 11.17 1 Vehicle Day 25-28 SCW 43.0 69.0 53.7 55.2 13.06 0.96 Example 2 (20 mg/kg) Day 25-28 SCW 3.2 25.6 4.5 11.1 12.57 0.010 Example 2 (50 mg/kg) Day 25-28 Key: RLU = relative light units; SCW = Streptococcal cell wall peptidoglycan-polysaccharide equivalent to 15 μg rhamnose/gram BW.

Crystallization and Data Collection

Crystals of apo proMMP9(29-444 ΔFnII) (SEQ ID NO:4) were grown by adding 1 microliter of protein to 1 microliter of a solution containing: 25% PEG 8K, 1% glycerol, 0.2 M Ammonium Sulfate, and 100 mM Sodium Cacodylate, pH 5.5. A cryoprotectant solution was prepared by the addition of 20% glycerol to a stabilizing solution. X-ray data of the apo proMMP9(29-444 ΔFnII) (SEQ ID NO:4) crystals were collected at ESRF beamline ID23 via the MXpress service. Crystals diffracted to 1.7 Å. Crystals formed in a space group C2 with unit cell dimensions: a=90.3 Å b=73.2 Å c=77.5 Å, β=106.3. The structure was solved by molecular replacement methods with the program EPMR (Kissinger, Gehlhaar et al. 1999) using the previously published proMMP9 structure as the search molecule for the proMMP9(29-444 ΔFnII) structure. Two molecules of proMMP9(29-444 ΔFnII) (SEQ ID NO:4) were found in the asymmetric unit. The data were refined with the program CNX. The R-factor was 20.9 R-free 23.2. The overall fold of the protein was very similar to published structure. The first residue visible in electron density at the N-terminus was Asp 41. N-terminal sequencing of crystals of the proMMP9(29-444 ΔFnII) (SEQ ID NO:4) protein showed that the N-terminal residue of the material that crystallized was Leu 35, which indicated that the proMMP9(29-444 ΔFn) (SEQ ID NO:4) protein was further processed at the N-terminus during expression, purification, or crystallization of the protein. Mass spectrometry of the purified protein confirmed that additional processing of the N-terminus had occurred during expression or purification. Thus the crystallized form of proMMP9 was actually proMMP9(35-444 ΔFnII) (SEQ ID NO:12).

Cocrystallization trials with Example 1 did not produce crystals. A data set derived from a 24 hour soak to produce a complex of apo proMMP9(35-444 ΔFnII) (SEQ ID NO:12) crystals with Example 1 (1 mM in 5% DMSO) was collected at the IMCA—CAT beamline at the Advanced Photon Source in Chicago. The crystal diffracted to 2.9 Å resolution. The data were refined with the program CNX. The structure has R-factor of 30.0 and R-free of 34.8. Initial electron density maps indicated the presence of inhibitor and a reordering of residues near Phe 107 in one molecule of the asymmetric unit. The changes in the protein were focused around residue 107 and did not propagate through the molecule (including the zinc binding sites).

Data sets were also collected for a number of other compounds that were soaked for 24 hours to produce complexes with proMMP9(35-444 ΔFnII) (SEQ ID NO:12). Data were collected with a Rigaku 007 HF generator and a Saturn 94 CCD detector. Data were processed with the d*trek program(Pflugrath 1999) and refined with the program Phenix(Adams, Grosse-Kunstleve et al. 2002). Relevant data collection statistics for selected data sets are found in Table 10. The programs Coot(Emsley and Cowtan 2004), Pymol (DeLano Scientific), and Quanta (Accelerys) were used for inspection of the electron density maps. Figures were generated with Pymol and Moe (Schrodinger).

TABLE 10 X-ray data collection and refinement statistics for apo and complexed proMMP9(35-444 ΔFnII) (SEQ ID NO: 12) apo Example 1 Space Group C2 C2 Unit Cell Parameters a (Å) 90.3 91.7 b (Å) 73.2 73.7 c (Å) 77.5 79.4 β (°) 106.3 105.4 Resolution Range (Å) 49-1.7 38-2.7 % Complete 98.1 (97.2) 99.7 (100)  R-sym 0.048 (0.181) 0.112 (0.325) Redundancy 3.2 3.6 Rfact/Rfree 20.9/23.2 27.9/34.9 Rmsd from ideal 0.0034 0.0088 bond length (Å) Rmsd from ideal 0.77 1.1 bond angle (°) Example 2 Example 3 Example 4 Space Group C2 C2 C2 Unit Cell Parameters a (Å) 90.7 91.0 90.0 b (Å) 73.0 73.6 77.1 c (Å) 78.2 78.0 75.0 β (°) 104.6 106.0 102.1 Resolution Range (Å) 29-2.0 49-2.6 29-2.8 % Complete 90.1 (78.2) 94.8 (92)   91.5 (84.5) R-sym 0.060 (0.226) 0.112 (0.325) 0.081 (0.301) Redundancy 2.1 3.6 3.1 Rfact/Rfree 25.0/30.1 27.6/35.6 21.9/29.1 Rmsd from ideal 0.008 0.007 0.0077 bond length (Å) Rmsd from ideal 1.3 1.1 0.87 bond angle (°)

X-ray Structure Discussion

The apo form of proMMP9(35-444 ΔFnII) (SEQ ID NO:12) was initially crystallized. The apo structure was determined at a much higher resolution (1.7 Å versus 2.5 Å) compared to the previously published proMMP9 structure that included the FnII domains (Elkins, Ho et al. 2002), but the structure of proMMP9(35-444 ΔFnII) (SEQ ID NO:12) was essentially identical for residues present in the form of the protein that included the FnII domains. Thus removal of FnII domains in the proMMP9(35-444 ΔFnII) (SEQ ID NO:12) structure did not alter the overall structure of the catalytic domain compared to the previously published full length structure. In particular, the backbone atoms of residues surrounding the residue Phe 107 cleavage site are in similar positions in the proMMP9(35-444 ΔFnII) (SEQ ID NO:12) structure and the previously published proMMP9 structure that included the FnII domains.

Binding of Example 1

The binding of Example 1 requires the reorientation of several residues in the pro region of proMMP9(35-444 ΔFnII) (SEQ ID NO:12). The phenoxy moiety of the inhibitor binds in a region of space that was occupied by Phe 107 in the apo protein. This location is 6 Å away from the structural zinc. Cys 99 blocks the area between the compound and the zinc, so that there is no direct access to the zinc from Example 1. No hydrogen bond is observed for the phenoxy oxygen, which suggests that the role of this group may be more important in altering the electronics of the aromatic ring than in a specific hydrogen bonding interaction. The residues that are in the vicinity of the phenoxy group include: Val 101, Pro 102, Tyr 179, H is 190 (coordinated to the structural zinc), and Phe 192. The inner thiazole ring of Example 1 is located near residues Phe 110 from the pro domain and His 405 (coordinated to the catalytic zinc). A 2.8 Å distance was observed between the thiazole sulfur and the backbone carbonyl of Ala 191. In the proMMP9(35-444 ΔFnII) (SEQ ID NO:12) structure in the absence of inhibitor, five solvent molecules occupy the space occupied by the two thiazole rings in the Example 1 structure. The terminal methyl thiazole ring is located near residues Leu 114 and Asp 410. Interestingly, the acetamide group is located in the same position as the guanidino group of Arg 108 in the apo proMMP9(35-444 ΔFnII) (SEQ ID NO:12) structure.

The interactions of Cys 99 (the cysteine switch) remain consistent between inhibited and uninhibited proMMP9(35-444 ΔFnII) (SEQ ID NO:12). There were no differences in the zinc coordination of either the catalytic or structural zinc ions. Indeed, the reorientations were concentrated in the region between residues 103 and 108.

Binding of Example 2

The binding of Example 2 requires the reorientation of several residues in the pro region of proMMP9(35-444 ΔFnII) (SEQ ID NO:12). The 1-methylethoxy-benzenesulfonamide moiety of the inhibitor binds in a region of space that was occupied by Phe 107 in the apo protein. This location is 6 Å away from the structural zinc. Cys 99 blocks the area between the compound and the zinc, so that there is no direct access to the zinc from Example 2. A hydrogen bonds is observed between the aniline NH and the carbonyl oxygen of Ala 191 in the protein. The sulphonamide also makes hydrogen bonds to the protein. The nitrogen bonds to the NH of Gly 105 and one of the oxygens forms bonds with the amide nitrogens of Phe 107 and Gln 108. The residues that are in the vicinity of the 1-methylethoxy-benzenesulfonamide group include: Gly 100, Val 101, Pro 102, Leu 104, Gly 105, Arg 106, Phe 107, Gln 108, Phe 110, Tyr 179, His 190 (coordinated to the structural zinc), Ala 191 and Phe 192. The inner thiazole ring of Example 2 is located near residues Pro 192 and His 405 (coordinated to the catalytic zinc). The outer thiazole ring of Example 2 is located near residues Arg 106, Leu 114 and Asp 410. These two thiazole rings make no direct hydrogen bonds with the protein.

Binding of Example 3

The binding of Example 3 requires the reorientation of several residues in the pro region of proMMP9(35-444 ΔFnII) (SEQ ID NO:12). The methoxybenzenamide moiety of the inhibitor binds in a region of space that was occupied by Phe 107 in the apo protein. This location is 6 Å away from the structural zinc. Cys 99 blocks the area between the compound and the zinc, so that there is no direct access to the zinc from Example 2. Hydrogen bonds are observed between the aniline NH and the carbonyl oxygen of Ala 191 in the protein. The amide also makes hydrogen bonds to the protein. The nitrogen bonds to the NH of Gly 105 and one of the oxygens forms bonds with the amide nitrogens of Phe 107 and Gln 108. The residues that are in the vicinity of the methoxybenzenamide group include: Gly 100, Val 101, Pro 102, Leu 104, Gly 105, Arg 106, Phe 107, Gln 108, Phe 110, Tyr 179, His 190 (coordinated to the structural zinc), Ala 191 and Phe 192. The inner thiazole ring of Example 3 is located near residues Pro 192 and His 405 (coordinated to the catalytic zinc). The outer thiazole ring of Example 2 is located near residues Arg 106, Leu 114 and Asp 410. These two thiazole rings make no direct hydrogen bonds with the protein.

Binding of Example 4

The binding of Example 4 requires the reorientation of several residues in the pro region of proMMP9(35-444 ΔFnII) (SEQ ID NO:12). The methoxy-pyridine moiety of the inhibitor binds in a region of space that was occupied by Phe 107 in the apo protein. This location is 6 Å away from the structural zinc. Cys 99 blocks the area between the compound and the zinc, so that there is no direct access to the zinc from Example 2. A hydrogen bond is observed between the aniline NH and the carbonyl oxygen of Ala 191 in the protein. The residues that are in the vicinity of the methoxy-pyridine group include: Val 101, Pro 102, Arg 106, Gln 108, Phe 110, Tyr 179, His 190 (coordinated to the structural zinc), Ala 191 and Phe 192. The methyl-imidazo-benzothiazole ring of Example 4 is located near residues Arg 106, Leu 114, Pro 192, His 405 (coordinated to the catalytic zinc) and Asp 410. This fused ring makes no direct hydrogen bonds with the protein.

A soak of any of the above compounds proved successful in showing electron density consistent with compound binding. The loop containing residues 103-108 reorganizes to accommodate compound binding. Sometimes the loop makes direct hydrogen bonds with the compound further stabilizing the interaction. The exact orientation of this loop is seen to vary in the complexes with the various compounds. In the case of Example 1, this loop remained disordered. Electron density for the entire loop was observed in the structures for Example 2, Example 3, and Example 4. The position of the displaced Phe 107 and the Arg 106 that make up the scissile bond cleaved to form the active enzyme is seen to vary dramatically between compound bound structures. The general effect is however to keep these residues from being cleaved.

As mentioned above, the phenoxy group binds in a pocket that is occupied by Phe 107 in the apo proMMP9(35-444 ΔFnII) (SEQ ID NO:12) structure. In essence, the aromatic ring of the inhibitor replaces the aromatic ring of the phenylalanine residue. In the mature enzyme, the pocket is occupied by Phe 110. In the structure of proMMP1, the residues of the cleavage site are disordered, however, a HEPES molecule is found to bind in the same region as these inhibitors.

Although proMMP9 can be activated by several different proteases, the compounds presented here must function by making proMMP9 a less optimal substrate. Data has shown that the compounds do not inhibit the catalytic activity of MMP3 or MMP9. It is possible that the compounds function by limiting the mobility of residues near the cleavage site. If these residues are stabilized in a conformation that does not allow proMMP9 to be a productive substrate, it would lead to inhibition of the activation. As mentioned earlier, Phe 110 occupies this location in the catalytically active protein. The binding of compound at this site may prevent Phe 110 from moving into this location which could be required for catalysis and activation. In addition to motion of Phe 107, in some structures Arg 106 is in a different environment and Asp 410 rotates to form a bidentate interaction with the side-chain of Arg 106. This salt bridge may serve to lock proMMP9 in a conformation that is not able serve as a productive substrate.

Allosteric Binding Site

The core of the allosteric binding site of proMMP9 is comprised of amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1). This site forms the binding surface that the key residue phenylalanine (Phe) 107 occupies in the “native” proenzyme. The allosteric processing inhibitors bind in this site and also interact with the displaced loop (residue 104-108) which forms the flap of the binding site. This loop is flexible and has a number of different conformations that can make contact and interact with the inhibitors. These interactions with the loop are inhibitor specific.

Selectivity

The selectivity of these compounds for all other MMPs is yet to be determined, but it is very likely that the compounds will have much better specificity than previous MMP inhibitors that bound in the active sites of the catalytically active enzymes. Structurally, the binding of these compounds requires the dramatic movement of several residues and the sequence identity of the pro domains of MMPs at the final cleavage site is significantly less than at the active site. Given the historic difficulty in producing selective MMP inhibitors that display favorable pharmacokinetic properties, it is a significant finding to identify compounds that inhibit the activation of a proMMP.

Modeling and Other MMPs

This method of inhibition should be transferable to other MMPs based on sequence alignment of the MMPs and modeling suggesting that other proMMPs could rearrange in a similar fashion to accommodate binding of activation inhibitors. The overall secondary structure of the pro region is conserved in the proMMPs. The tertiary structure for the pro domains is a four helical bundle in the determined structures and predicted to have the same fold from the sequences for the remaining MMPs. In addition, the proMMPs have a similar pocket for the binding of the cysteine switch and while there are a variety of residues that fill the cavity in the catalytic domain the general mode of stabilization will remain the same.

Of note is the structure of proMMP1, where the region is disordered in the area of the cleavage site, suggesting that these residues are flexible. In addition, both MMP1 and MMP3, which are cleaved to the active form by MMP3, have a cleavage site that contains an S1 hydrophilic residue and a S1′ Phe residue. Indeed, the proMMP3 structure has the S1′ Phe in a very similar location to Phe 107 in the apo proMMP9 structure. FIG. 7 shows the overlap of all current proMMP structures, (MMP9 (pdb1L6J), MMP1 (pdb1SU3), and MMP2 (pdb1CK7)). A sequence alignment of the pro domains for the MMP family is shown in FIG. 8.

Evidence that this method of inhibition is in fact transferable to other MMPs was demonstrated with a number of compounds that showed activity in inhibiting activation of both proMMP9 and proMMP13. See for example, Table 2, showing that Example 2 inhibited activation of both proMMP9 and proMMP13. Furthermore, it was also demonstrated with ThermoFluor® that a number of compounds bind to both proMMP9 and proMMP13. See for example, Table 1, showing ThermoFluor® data for selected compounds using proMM9 and proMMP13.

Coordinates

Tables 11, 12, 13, and 14, list the coordinates for representative structures of proMMP9 complexed with examples of different allosteric processing inhibitors. Table 15 lists the coordinates for the apo form of proMMP9.

TABLE 11 Coordinates for pro MMP9(35-444 ΔFnII) (SEQ ID NO: 12) complex with Example 1 ATOM 1801 CB ASP B 41 −5.622 13.523 78.580 1.00 62.75 B C ATOM 1802 CG ASP B 41 −6.779 14.221 77.898 1.00 63.89 B C ATOM 1803 OD1 ASP B 41 −7.191 13.757 76.812 1.00 64.66 B O ATOM 1804 OD2 ASP B 41 −7.271 15.235 78.447 1.00 64.07 B O ATOM 1805 C ASP B 41 −4.493 15.705 78.723 1.00 62.33 B C ATOM 1806 O ASP B 41 −3.955 16.589 78.066 1.00 63.96 B O ATOM 1807 N ASP B 41 −3.222 13.602 79.148 1.00 61.28 B N ATOM 1808 CA ASP B 41 −4.305 14.244 78.357 1.00 61.88 B C ATOM 1809 N ARG B 42 −5.273 15.963 79.766 1.00 62.29 B N ATOM 1810 CA ARG B 42 −5.474 17.334 80.222 1.00 62.94 B C ATOM 1811 CB ARG B 42 −6.406 17.366 81.435 1.00 62.27 B C ATOM 1812 CG ARG B 42 −6.403 18.686 82.180 1.00 60.80 B C ATOM 1813 CD ARG B 42 −7.548 18.762 83.172 1.00 61.00 B C ATOM 1814 NE ARG B 42 −7.787 20.139 83.599 1.00 61.72 B N ATOM 1815 CZ ARG B 42 −8.797 20.900 83.181 1.00 62.56 B C ATOM 1816 NH1 ARG B 42 −9.683 20.418 82.315 1.00 60.84 B N ATOM 1817 NH2 ARG B 42 −8.912 22.151 83.627 1.00 63.72 B N ATOM 1818 C ARG B 42 −4.135 17.945 80.603 1.00 63.83 B C ATOM 1819 O ARG B 42 −3.902 19.144 80.411 1.00 63.99 B O ATOM 1820 N GLN B 43 −3.255 17.108 81.150 1.00 63.14 B N ATOM 1821 CA GLN B 43 −1.942 17.566 81.587 1.00 62.24 B C ATOM 1822 CB GLN B 43 −1.111 16.375 82.081 1.00 64.08 B C ATOM 1823 CG GLN B 43 −1.834 15.462 83.078 1.00 65.58 B C ATOM 1824 CD GLN B 43 −2.663 14.370 82.398 1.00 66.13 B C ATOM 1825 OE1 GLN B 43 −2.140 13.581 81.597 1.00 66.23 B O ATOM 1826 NE2 GLN B 43 −3.958 14.318 82.719 1.00 64.68 B N ATOM 1827 C GLN B 43 −1.263 18.232 80.395 1.00 61.38 B C ATOM 1828 O GLN B 43 −0.720 19.338 80.503 1.00 60.88 B O ATOM 1829 N LEU B 44 −1.321 17.547 79.254 1.00 60.44 B N ATOM 1830 CA LEU B 44 −0.887 18.113 77.981 1.00 60.89 B C ATOM 1831 CB LEU B 44 −1.102 17.117 76.836 1.00 59.48 B C ATOM 1832 CG LEU B 44 −1.197 17.711 75.422 1.00 59.18 B C ATOM 1833 CD1 LEU B 44 0.055 18.519 75.088 1.00 59.52 B C ATOM 1834 CD2 LEU B 44 −1.384 16.586 74.422 1.00 58.19 B C ATOM 1835 C LEU B 44 −1.687 19.362 77.679 1.00 61.53 B C ATOM 1836 O LEU B 44 −1.161 20.356 77.176 1.00 61.91 B O ATOM 1837 N ALA B 45 −2.974 19.296 77.980 1.00 61.27 B N ATOM 1838 CA ALA B 45 −3.876 20.347 77.572 1.00 62.45 B C ATOM 1839 CB ALA B 45 −5.315 19.979 77.940 1.00 63.46 B C ATOM 1840 C ALA B 45 −3.465 21.626 78.264 1.00 62.12 B C ATOM 1841 O ALA B 45 −3.493 22.711 77.674 1.00 62.26 B O ATOM 1842 N GLU B 46 −3.064 21.490 79.519 1.00 62.06 B N ATOM 1843 CA GLU B 46 −2.748 22.647 80.330 1.00 61.09 B C ATOM 1844 CB GLU B 46 −2.990 22.331 81.802 1.00 62.73 B C ATOM 1845 CG GLU B 46 −4.414 21.904 82.110 1.00 63.16 B C ATOM 1846 CD GLU B 46 −4.571 21.442 83.542 1.00 64.25 B C ATOM 1847 OE1 GLU B 46 −5.539 21.882 84.202 1.00 64.03 B O ATOM 1848 OE2 GLU B 46 −3.724 20.642 84.005 1.00 64.81 B O ATOM 1849 C GLU B 46 −1.304 23.036 80.107 1.00 59.85 B C ATOM 1850 O GLU B 46 −0.972 24.222 80.103 1.00 59.39 B O ATOM 1851 N GLU B 47 −0.447 22.040 79.905 1.00 58.45 B N ATOM 1852 CA GLU B 47 0.961 22.316 79.632 1.00 58.81 B C ATOM 1853 CB GLU B 47 1.738 21.004 79.459 1.00 60.80 B C ATOM 1854 CG GLU B 47 3.048 20.921 80.257 1.00 62.91 B C ATOM 1855 CD GLU B 47 4.243 21.574 79.565 1.00 64.06 B C ATOM 1856 OE1 GLU B 47 4.785 20.983 78.599 1.00 64.66 B O ATOM 1857 OE2 GLU B 47 4.649 22.677 80.000 1.00 64.03 B O ATOM 1858 C GLU B 47 1.096 23.175 78.364 1.00 57.20 B C ATOM 1859 O GLU B 47 1.731 24.229 78.388 1.00 56.69 B O ATOM 1860 N TYR B 48 0.477 22.713 77.274 1.00 54.95 B N ATOM 1861 CA TYR B 48 0.540 23.372 75.966 1.00 51.46 B C ATOM 1862 CB TYR B 48 −0.245 22.567 74.929 1.00 50.46 B C ATOM 1863 CG TYR B 48 −0.016 22.980 73.488 1.00 48.44 B C ATOM 1864 CD1 TYR B 48 −0.555 24.157 72.988 1.00 47.77 B C ATOM 1865 CE1 TYR B 48 −0.387 24.518 71.665 1.00 47.69 B C ATOM 1866 CD2 TYR B 48 0.708 22.167 72.617 1.00 46.99 B C ATOM 1867 CE2 TYR B 48 0.883 22.518 71.282 1.00 46.69 B C ATOM 1868 CZ TYR B 48 0.324 23.702 70.814 1.00 47.29 B C ATOM 1869 OH TYR B 48 0.432 24.077 69.494 1.00 46.46 B O ATOM 1870 C TYR B 48 0.006 24.797 75.992 1.00 51.37 B C ATOM 1871 O TYR B 48 0.589 25.693 75.385 1.00 51.99 B O ATOM 1872 N LEU B 49 −1.101 25.017 76.685 1.00 50.67 B N ATOM 1873 CA LEU B 49 −1.577 26.371 76.830 1.00 50.62 B C ATOM 1874 CB LEU B 49 −2.924 26.403 77.544 1.00 50.69 B C ATOM 1875 CG LEU B 49 −4.068 25.775 76.745 1.00 50.22 B C ATOM 1876 CD1 LEU B 49 −5.359 25.742 77.563 1.00 50.84 B C ATOM 1877 CD2 LEU B 49 −4.268 26.584 75.491 1.00 51.85 B C ATOM 1878 C LEU B 49 −0.556 27.208 77.586 1.00 50.99 B C ATOM 1879 O LEU B 49 −0.175 28.282 77.123 1.00 52.52 B O ATOM 1880 N TYR B 50 −0.088 26.740 78.735 1.00 50.56 B N ATOM 1881 CA TYR B 50 0.806 27.589 79.513 1.00 52.06 B C ATOM 1882 CB TYR B 50 1.215 26.909 80.849 1.00 54.75 B C ATOM 1883 CG TYR B 50 2.356 27.610 81.595 1.00 56.49 B C ATOM 1884 CD1 TYR B 50 2.132 28.749 82.369 1.00 56.67 B C ATOM 1885 CE1 TYR B 50 3.196 29.425 82.983 1.00 57.25 B C ATOM 1886 CD2 TYR B 50 3.669 27.165 81.465 1.00 57.57 B C ATOM 1887 CE2 TYR B 50 4.733 27.833 82.071 1.00 57.73 B C ATOM 1888 CZ TYR B 50 4.492 28.962 82.822 1.00 57.73 B C ATOM 1889 OH TYR B 50 5.556 29.647 83.366 1.00 57.23 B O ATOM 1890 C TYR B 50 2.046 27.888 78.666 1.00 51.21 B C ATOM 1891 O TYR B 50 2.565 29.010 78.658 1.00 50.09 B O ATOM 1892 N ARG B 51 2.490 26.874 77.929 1.00 50.13 B N ATOM 1893 CA ARG B 51 3.795 26.897 77.285 1.00 49.14 B C ATOM 1894 CB ARG B 51 4.092 25.520 76.658 1.00 49.01 B C ATOM 1895 CG ARG B 51 5.358 25.464 75.799 1.00 49.48 B C ATOM 1896 CD ARG B 51 5.841 24.031 75.496 1.00 49.62 B C ATOM 1897 NE ARG B 51 6.502 23.367 76.633 1.00 50.14 B N ATOM 1898 CZ ARG B 51 7.815 23.369 76.872 1.00 49.61 B C ATOM 1899 NH1 ARG B 51 8.656 24.004 76.064 1.00 50.15 B N ATOM 1900 NH2 ARG B 51 8.289 22.716 77.921 1.00 49.36 B N ATOM 1901 C ARG B 51 3.872 27.995 76.229 1.00 48.42 B C ATOM 1902 O ARG B 51 4.867 28.708 76.133 1.00 46.51 B O ATOM 1903 N TYR B 52 2.817 28.146 75.443 1.00 47.18 B N ATOM 1904 CA TYR B 52 2.913 29.024 74.292 1.00 48.85 B C ATOM 1905 CB TYR B 52 2.407 28.290 73.038 1.00 47.39 B C ATOM 1906 CG TYR B 52 3.175 27.018 72.746 1.00 44.63 B C ATOM 1907 CD1 TYR B 52 2.580 25.777 72.910 1.00 44.87 B C ATOM 1908 CE1 TYR B 52 3.286 24.609 72.683 1.00 44.91 B C ATOM 1909 CD2 TYR B 52 4.504 27.061 72.342 1.00 43.90 B C ATOM 1910 CE2 TYR B 52 5.227 25.900 72.108 1.00 43.90 B C ATOM 1911 CZ TYR B 52 4.615 24.669 72.279 1.00 44.52 B C ATOM 1912 OH TYR B 52 5.313 23.494 72.040 1.00 43.22 B O ATOM 1913 C TYR B 52 2.162 30.328 74.533 1.00 49.58 B C ATOM 1914 O TYR B 52 1.683 30.977 73.597 1.00 49.81 B O ATOM 1915 N GLY B 53 2.070 30.691 75.815 1.00 51.04 B N ATOM 1916 CA GLY B 53 1.646 32.024 76.217 1.00 50.61 B C ATOM 1917 C GLY B 53 0.183 32.203 76.596 1.00 51.60 B C ATOM 1918 O GLY B 53 −0.182 33.267 77.088 1.00 51.76 B O ATOM 1919 N TYR B 54 −0.654 31.189 76.378 1.00 51.15 B N ATOM 1920 CA TYR B 54 −2.090 31.419 76.355 1.00 51.50 B C ATOM 1921 CB TYR B 54 −2.832 30.230 75.729 1.00 51.54 B C ATOM 1922 CG TYR B 54 −2.587 30.086 74.230 1.00 53.01 B C ATOM 1923 CD1 TYR B 54 −1.779 29.071 73.732 1.00 53.74 B C ATOM 1924 CE1 TYR B 54 −1.511 28.958 72.383 1.00 53.90 B C ATOM 1925 CD2 TYR B 54 −3.126 30.990 73.317 1.00 53.57 B C ATOM 1926 CE2 TYR B 54 −2.857 30.879 71.960 1.00 54.75 B C ATOM 1927 CZ TYR B 54 −2.048 29.857 71.508 1.00 54.89 B C ATOM 1928 OH TYR B 54 −1.767 29.728 70.171 1.00 56.35 B O ATOM 1929 C TYR B 54 −2.646 31.711 77.727 1.00 52.70 B C ATOM 1930 O TYR B 54 −3.155 32.801 77.977 1.00 52.64 B O ATOM 1931 N THR B 55 −2.546 30.741 78.623 1.00 55.09 B N ATOM 1932 CA THR B 55 −3.071 30.908 79.968 1.00 56.46 B C ATOM 1933 CB THR B 55 −2.798 29.652 80.782 1.00 55.37 B C ATOM 1934 OG1 THR B 55 −1.395 29.404 80.821 1.00 56.74 B O ATOM 1935 CG2 THR B 55 −3.464 28.459 80.123 1.00 56.02 B C ATOM 1936 C THR B 55 −2.463 32.152 80.632 1.00 57.54 B C ATOM 1937 O THR B 55 −3.126 32.853 81.401 1.00 58.41 B O ATOM 1938 N ARG B 56 −1.212 32.453 80.303 1.00 58.28 B N ATOM 1939 CA ARG B 56 −0.594 33.689 80.772 1.00 59.32 B C ATOM 1940 CB ARG B 56 0.835 33.788 80.240 1.00 61.48 B C ATOM 1941 CG ARG B 56 1.292 35.221 80.010 1.00 64.60 B C ATOM 1942 CD ARG B 56 2.554 35.538 80.798 1.00 66.20 B C ATOM 1943 NE ARG B 56 2.845 36.971 80.804 1.00 65.83 B N ATOM 1944 CZ ARG B 56 3.769 37.554 80.047 1.00 65.50 B C ATOM 1945 NH1 ARG B 56 4.502 36.823 79.208 1.00 63.11 B N ATOM 1946 NH2 ARG B 56 3.962 38.868 80.143 1.00 63.67 B N ATOM 1947 C ARG B 56 −1.381 34.940 80.350 1.00 58.31 B C ATOM 1948 O ARG B 56 −1.627 35.818 81.160 1.00 58.35 B O ATOM 1949 N VAL B 57 −1.768 35.014 79.079 1.00 58.36 B N ATOM 1950 CA VAL B 57 −2.421 36.204 78.528 1.00 56.57 B C ATOM 1951 CB VAL B 57 −2.555 36.105 76.964 1.00 55.30 B C ATOM 1952 CG1 VAL B 57 −3.465 37.191 76.423 1.00 54.65 B C ATOM 1953 CG2 VAL B 57 −1.181 36.227 76.311 1.00 52.96 B C ATOM 1954 C VAL B 57 −3.803 36.421 79.140 1.00 57.00 B C ATOM 1955 O VAL B 57 −4.108 37.520 79.608 1.00 57.15 B O ATOM 1956 N ALA B 58 −4.626 35.371 79.141 1.00 57.18 B N ATOM 1957 CA ALA B 58 −5.993 35.453 79.651 1.00 57.73 B C ATOM 1958 CB ALA B 58 −6.619 34.059 79.691 1.00 56.30 B C ATOM 1959 C ALA B 58 −6.059 36.112 81.040 1.00 58.36 B C ATOM 1960 O ALA B 58 −7.092 36.671 81.427 1.00 58.49 B O ATOM 1961 N GLU B 59 −4.956 36.053 81.783 1.00 59.14 B N ATOM 1962 CA GLU B 59 −4.819 36.823 83.021 1.00 59.00 B C ATOM 1963 CB GLU B 59 −3.702 36.228 83.897 1.00 59.61 B C ATOM 1964 CG GLU B 59 −3.785 34.713 84.100 1.00 59.48 B C ATOM 1965 CD GLU B 59 −2.454 34.084 84.515 1.00 60.05 B C ATOM 1966 OE1 GLU B 59 −1.426 34.801 84.552 1.00 60.10 B O ATOM 1967 OE2 GLU B 59 −2.433 32.864 84.803 1.00 60.25 B O ATOM 1968 C GLU B 59 −4.489 38.290 82.705 1.00 59.68 B C ATOM 1969 O GLU B 59 −5.250 38.994 82.033 1.00 59.54 B O ATOM 1970 N GLY B 68 −10.715 26.983 79.395 1.00 60.34 B N ATOM 1971 CA GLY B 68 −11.961 27.302 78.719 1.00 62.09 B C ATOM 1972 C GLY B 68 −11.886 28.595 77.927 1.00 63.65 B C ATOM 1973 O GLY B 68 −12.057 28.587 76.701 1.00 64.44 B O ATOM 1974 N PRO B 69 −11.637 29.733 78.605 1.00 64.13 B N ATOM 1975 CD PRO B 69 −11.735 29.893 80.067 1.00 62.87 B C ATOM 1976 CA PRO B 69 −11.362 31.018 77.943 1.00 63.98 B C ATOM 1977 CB PRO B 69 −11.242 32.011 79.106 1.00 62.94 B C ATOM 1978 CG PRO B 69 −11.969 31.373 80.221 1.00 62.18 B C ATOM 1979 C PRO B 69 −10.081 30.962 77.115 1.00 63.67 B C ATOM 1980 O PRO B 69 −10.112 31.166 75.908 1.00 64.56 B O ATOM 1981 N ALA B 70 −8.956 30.678 77.766 1.00 63.29 B N ATOM 1982 CA ALA B 70 −7.683 30.598 77.055 1.00 63.79 B C ATOM 1983 CB ALA B 70 −6.512 30.560 78.041 1.00 61.38 B C ATOM 1984 C ALA B 70 −7.621 29.393 76.105 1.00 63.72 B C ATOM 1985 O ALA B 70 −6.629 29.212 75.404 1.00 63.83 B O ATOM 1986 N LEU B 71 −8.673 28.574 76.076 1.00 62.11 B N ATOM 1987 CA LEU B 71 −8.763 27.502 75.090 1.00 60.75 B C ATOM 1988 CB LEU B 71 −9.712 26.404 75.574 1.00 60.83 B C ATOM 1989 CG LEU B 71 −9.207 24.967 75.365 1.00 61.47 B C ATOM 1990 CD1 LEU B 71 −10.006 24.256 74.294 1.00 60.61 B C ATOM 1991 CD2 LEU B 71 −7.730 25.003 75.008 1.00 61.49 B C ATOM 1992 C LEU B 71 −9.244 28.046 73.739 1.00 61.00 B C ATOM 1993 O LEU B 71 −9.076 27.405 72.698 1.00 61.47 B O ATOM 1994 N LEU B 72 −9.847 29.234 73.761 1.00 61.08 B N ATOM 1995 CA LEU B 72 −10.315 29.898 72.541 1.00 59.16 B C ATOM 1996 CB LEU B 72 −11.565 30.739 72.834 1.00 58.95 B C ATOM 1997 CG LEU B 72 −12.880 30.283 72.191 1.00 58.78 B C ATOM 1998 CD1 LEU B 72 −13.748 31.487 71.866 1.00 57.47 B C ATOM 1999 CD2 LEU B 72 −12.577 29.518 70.926 1.00 60.36 B C ATOM 2000 C LEU B 72 −9.236 30.795 71.913 1.00 58.54 B C ATOM 2001 O LEU B 72 −9.124 30.874 70.694 1.00 58.48 B O ATOM 2002 N LEU B 73 −8.444 31.468 72.741 1.00 56.65 B N ATOM 2003 CA LEU B 73 −7.310 32.210 72.224 1.00 55.43 B C ATOM 2004 CB LEU B 73 −6.502 32.817 73.357 1.00 53.30 B C ATOM 2005 CG LEU B 73 −7.100 34.083 73.926 1.00 51.80 B C ATOM 2006 CD1 LEU B 73 −5.989 34.855 74.597 1.00 52.00 B C ATOM 2007 CD2 LEU B 73 −7.728 34.914 72.828 1.00 50.38 B C ATOM 2008 C LEU B 73 −6.392 31.335 71.380 1.00 56.07 B C ATOM 2009 O LEU B 73 −5.778 31.812 70.424 1.00 57.01 B O ATOM 2010 N LEU B 74 −6.287 30.058 71.735 1.00 55.82 B N ATOM 2011 CA LEU B 74 −5.412 29.147 71.002 1.00 55.30 B C ATOM 2012 CB LEU B 74 −4.950 27.985 71.896 1.00 52.49 B C ATOM 2013 CG LEU B 74 −4.395 26.749 71.174 1.00 49.44 B C ATOM 2014 CD1 LEU B 74 −3.361 26.095 72.027 1.00 47.93 B C ATOM 2015 CD2 LEU B 74 −5.518 25.774 70.857 1.00 48.17 B C ATOM 2016 C LEU B 74 −6.090 28.588 69.759 1.00 56.92 B C ATOM 2017 O LEU B 74 −5.429 28.302 68.752 1.00 57.25 B O ATOM 2018 N GLN B 75 −7.405 28.418 69.830 1.00 56.80 B N ATOM 2019 CA GLN B 75 −8.160 27.957 68.671 1.00 57.63 B C ATOM 2020 CB GLN B 75 −9.559 27.514 69.111 1.00 56.50 B C ATOM 2021 CG GLN B 75 −9.552 26.237 69.929 1.00 56.07 B C ATOM 2022 CD GLN B 75 −10.933 25.881 70.474 1.00 57.52 B C ATOM 2023 OE1 GLN B 75 −11.716 26.768 70.851 1.00 57.77 B O ATOM 2024 NE2 GLN B 75 −11.240 24.580 70.524 1.00 56.66 B N ATOM 2025 C GLN B 75 −8.236 29.058 67.600 1.00 57.80 B C ATOM 2026 O GLN B 75 −8.572 28.794 66.440 1.00 58.35 B O ATOM 2027 N LYS B 76 −7.881 30.282 67.997 1.00 56.87 B N ATOM 2028 CA LYS B 76 −7.963 31.452 67.123 1.00 56.29 B C ATOM 2029 CB LYS B 76 −8.367 32.693 67.938 1.00 57.72 B C ATOM 2030 CG LYS B 76 −9.383 33.608 67.242 1.00 58.97 B C ATOM 2031 CD LYS B 76 −10.044 34.604 68.214 1.00 59.88 B C ATOM 2032 CE LYS B 76 −11.231 33.982 68.981 1.00 60.17 B C ATOM 2033 NZ LYS B 76 −11.959 34.948 69.872 1.00 56.84 B N ATOM 2034 C LYS B 76 −6.653 31.728 66.371 1.00 55.13 B C ATOM 2035 O LYS B 76 −6.668 32.137 65.209 1.00 54.25 B O ATOM 2036 N GLN B 77 −5.521 31.488 67.022 1.00 54.38 B N ATOM 2037 CA GLN B 77 −4.224 31.627 66.359 1.00 53.88 B C ATOM 2038 CB GLN B 77 −3.118 31.716 67.407 1.00 54.27 B C ATOM 2039 CG GLN B 77 −3.404 32.753 68.460 1.00 58.53 B C ATOM 2040 CD GLN B 77 −3.526 34.158 67.870 1.00 60.95 B C ATOM 2041 OE1 GLN B 77 −4.583 34.554 67.329 1.00 60.29 B O ATOM 2042 NE2 GLN B 77 −2.434 34.924 67.968 1.00 62.21 B N ATOM 2043 C GLN B 77 −3.913 30.489 65.378 1.00 52.74 B C ATOM 2044 O GLN B 77 −3.192 30.685 64.410 1.00 52.34 B O ATOM 2045 N LEU B 78 −4.451 29.302 65.628 1.00 53.59 B N ATOM 2046 CA LEU B 78 −4.130 28.140 64.805 1.00 53.81 B C ATOM 2047 CB LEU B 78 −3.951 26.893 65.675 1.00 53.42 B C ATOM 2048 CG LEU B 78 −3.081 27.072 66.928 1.00 53.99 B C ATOM 2049 CD1 LEU B 78 −3.023 25.774 67.715 1.00 54.97 B C ATOM 2050 CD2 LEU B 78 −1.686 27.524 66.524 1.00 52.88 B C ATOM 2051 C LEU B 78 −5.271 27.917 63.839 1.00 54.05 B C ATOM 2052 O LEU B 78 −5.343 26.891 63.162 1.00 53.06 B O ATOM 2053 N SER B 79 −6.176 28.890 63.801 1.00 54.86 B N ATOM 2054 CA SER B 79 −7.328 28.834 62.913 1.00 55.94 B C ATOM 2055 CB SER B 79 −6.885 29.053 61.461 1.00 55.19 B C ATOM 2056 OG SER B 79 −6.458 30.397 61.262 1.00 51.79 B O ATOM 2057 C SER B 79 −8.045 27.498 63.063 1.00 56.76 B C ATOM 2058 O SER B 79 −8.404 26.855 62.072 1.00 56.92 B O ATOM 2059 N LEU B 80 −8.248 27.093 64.318 1.00 57.68 B N ATOM 2060 CA LEU B 80 −9.006 25.884 64.654 1.00 58.01 B C ATOM 2061 CB LEU B 80 −8.529 25.326 65.991 1.00 57.13 B C ATOM 2062 CG LEU B 80 −7.137 24.718 65.959 1.00 57.11 B C ATOM 2063 CD1 LEU B 80 −6.619 24.572 67.377 1.00 56.46 B C ATOM 2064 CD2 LEU B 80 −7.188 23.376 65.237 1.00 56.74 B C ATOM 2065 C LEU B 80 −10.506 26.140 64.739 1.00 58.76 B C ATOM 2066 O LEU B 80 −10.945 27.273 64.925 1.00 58.40 B O ATOM 2067 N PRO B 81 −11.317 25.080 64.604 1.00 60.19 B N ATOM 2068 CD PRO B 81 −11.022 23.717 64.125 1.00 60.96 B C ATOM 2069 CA PRO B 81 −12.726 25.240 64.962 1.00 61.92 B C ATOM 2070 CB PRO B 81 −13.283 23.824 64.829 1.00 61.57 B C ATOM 2071 CG PRO B 81 −12.377 23.164 63.824 1.00 60.13 B C ATOM 2072 C PRO B 81 −12.822 25.785 66.389 1.00 62.95 B C ATOM 2073 O PRO B 81 −12.367 25.138 67.341 1.00 63.10 B O ATOM 2074 N GLU B 82 −13.408 26.979 66.520 1.00 63.96 B N ATOM 2075 CA GLU B 82 −13.388 27.764 67.766 1.00 64.28 B C ATOM 2076 CB GLU B 82 −13.556 29.252 67.433 1.00 65.33 B C ATOM 2077 CG GLU B 82 −12.364 29.834 66.688 1.00 68.08 B C ATOM 2078 CD GLU B 82 −12.538 31.302 66.311 1.00 70.16 B C ATOM 2079 OE1 GLU B 82 −13.617 31.869 66.588 1.00 70.59 B O ATOM 2080 OE2 GLU B 82 −11.589 31.890 65.733 1.00 71.70 B O ATOM 2081 C GLU B 82 −14.447 27.331 68.789 1.00 64.05 B C ATOM 2082 O GLU B 82 −15.299 28.123 69.204 1.00 63.04 B O ATOM 2083 N THR B 83 −14.368 26.068 69.206 1.00 63.97 B N ATOM 2084 CA THR B 83 −15.416 25.456 70.015 1.00 63.61 B C ATOM 2085 CB THR B 83 −15.240 23.912 70.085 1.00 61.81 B C ATOM 2086 OG1 THR B 83 −13.957 23.590 70.643 1.00 62.11 B O ATOM 2087 CG2 THR B 83 −15.345 23.312 68.698 1.00 59.20 B C ATOM 2088 C THR B 83 −15.429 26.032 71.430 1.00 64.78 B C ATOM 2089 O THR B 83 −16.306 26.823 71.784 1.00 64.95 B O ATOM 2090 N GLY B 84 −14.446 25.653 72.233 1.00 65.43 B N ATOM 2091 CA GLY B 84 −14.503 25.989 73.641 1.00 67.36 B C ATOM 2092 C GLY B 84 −14.296 24.766 74.510 1.00 68.60 B C ATOM 2093 O GLY B 84 −14.476 24.825 75.722 1.00 69.36 B O ATOM 2094 N GLU B 85 −13.918 23.652 73.898 1.00 68.54 B N ATOM 2095 CA GLU B 85 −13.504 22.503 74.673 1.00 68.99 B C ATOM 2096 CB GLU B 85 −14.614 21.453 74.734 1.00 71.41 B C ATOM 2097 CG GLU B 85 −15.896 21.941 75.384 1.00 74.07 B C ATOM 2098 CD GLU B 85 −16.716 22.769 74.430 1.00 75.29 B C ATOM 2099 OE1 GLU B 85 −16.540 22.567 73.202 1.00 74.87 B O ATOM 2100 OE2 GLU B 85 −17.523 23.612 74.905 1.00 77.08 B O ATOM 2101 C GLU B 85 −12.268 21.873 74.088 1.00 68.03 B C ATOM 2102 O GLU B 85 −11.913 22.139 72.941 1.00 67.91 B O ATOM 2103 N LEU B 86 −11.617 21.033 74.888 1.00 68.12 B N ATOM 2104 CA LEU B 86 −10.596 20.118 74.386 1.00 68.46 B C ATOM 2105 CB LEU B 86 −9.919 19.384 75.545 1.00 67.76 B C ATOM 2106 CG LEU B 86 −9.158 20.199 76.590 1.00 69.11 B C ATOM 2107 CD1 LEU B 86 −8.581 19.262 77.647 1.00 68.81 B C ATOM 2108 CD2 LEU B 86 −8.042 20.986 75.925 1.00 69.76 B C ATOM 2109 C LEU B 86 −11.224 19.094 73.439 1.00 68.37 B C ATOM 2110 O LEU B 86 −11.431 17.937 73.812 1.00 68.45 B O ATOM 2111 N ASP B 87 −11.523 19.524 72.214 1.00 68.42 B N ATOM 2112 CA ASP B 87 −12.189 18.658 71.243 1.00 68.29 B C ATOM 2113 CB ASP B 87 −13.115 19.478 70.331 1.00 69.23 B C ATOM 2114 CG ASP B 87 −12.384 20.100 69.150 1.00 70.44 B C ATOM 2115 OD1 ASP B 87 −11.682 21.124 69.342 1.00 71.40 B O ATOM 2116 OD2 ASP B 87 −12.519 19.561 68.028 1.00 69.66 B O ATOM 2117 C ASP B 87 −11.166 17.906 70.397 1.00 67.76 B C ATOM 2118 O ASP B 87 −9.971 18.189 70.449 1.00 68.23 B O ATOM 2119 N SER B 88 −11.640 16.948 69.616 1.00 66.27 B N ATOM 2120 CA SER B 88 −10.745 16.148 68.807 1.00 65.89 B C ATOM 2121 CB SER B 88 −11.562 15.206 67.919 1.00 65.38 B C ATOM 2122 OG SER B 88 −10.746 14.217 67.324 1.00 66.14 B O ATOM 2123 C SER B 88 −9.817 17.032 67.952 1.00 65.57 B C ATOM 2124 O SER B 88 −8.677 16.661 67.694 1.00 65.55 B O ATOM 2125 N ALA B 89 −10.287 18.200 67.523 1.00 64.38 B N ATOM 2126 CA ALA B 89 −9.466 19.052 66.666 1.00 64.16 B C ATOM 2127 CB ALA B 89 −10.288 20.201 66.094 1.00 64.16 B C ATOM 2128 C ALA B 89 −8.310 19.609 67.466 1.00 64.27 B C ATOM 2129 O ALA B 89 −7.140 19.309 67.204 1.00 65.09 B O ATOM 2130 N THR B 90 −8.647 20.428 68.454 1.00 63.40 B N ATOM 2131 CA THR B 90 −7.634 21.062 69.283 1.00 61.60 B C ATOM 2132 CB THR B 90 −8.265 21.824 70.453 1.00 60.90 B C ATOM 2133 OG1 THR B 90 −9.263 22.727 69.962 1.00 61.09 B O ATOM 2134 CG2 THR B 90 −7.196 22.606 71.193 1.00 59.84 B C ATOM 2135 C THR B 90 −6.733 19.985 69.859 1.00 60.76 B C ATOM 2136 O THR B 90 −5.541 20.205 70.039 1.00 61.25 B O ATOM 2137 N LEU B 91 −7.318 18.822 70.142 1.00 60.27 B N ATOM 2138 CA LEU B 91 −6.615 17.747 70.832 1.00 59.27 B C ATOM 2139 CB LEU B 91 −7.592 16.630 71.212 1.00 58.33 B C ATOM 2140 CG LEU B 91 −7.413 15.944 72.573 1.00 57.71 B C ATOM 2141 CD1 LEU B 91 −7.680 16.952 73.663 1.00 57.34 B C ATOM 2142 CD2 LEU B 91 −8.372 14.771 72.711 1.00 57.54 B C ATOM 2143 C LEU B 91 −5.545 17.206 69.893 1.00 59.31 B C ATOM 2144 O LEU B 91 −4.561 16.598 70.323 1.00 57.85 B O ATOM 2145 N LYS B 92 −5.745 17.439 68.600 1.00 59.01 B N ATOM 2146 CA LYS B 92 −4.753 17.059 67.614 1.00 59.15 B C ATOM 2147 CB LYS B 92 −5.408 16.746 66.260 1.00 60.11 B C ATOM 2148 CG LYS B 92 −4.532 15.902 65.315 1.00 61.79 B C ATOM 2149 CD LYS B 92 −5.043 15.942 63.865 1.00 62.34 B C ATOM 2150 CE LYS B 92 −3.922 16.193 62.854 1.00 61.30 B C ATOM 2151 NZ LYS B 92 −4.480 16.472 61.504 1.00 61.09 B N ATOM 2152 C LYS B 92 −3.750 18.188 67.455 1.00 58.04 B C ATOM 2153 O LYS B 92 −2.541 17.950 67.379 1.00 59.11 B O ATOM 2154 N ALA B 93 −4.233 19.422 67.419 1.00 56.13 B N ATOM 2155 CA ALA B 93 −3.320 20.536 67.208 1.00 55.38 B C ATOM 2156 CB ALA B 93 −4.052 21.868 67.404 1.00 54.41 B C ATOM 2157 C ALA B 93 −2.146 20.426 68.182 1.00 54.25 B C ATOM 2158 O ALA B 93 −0.984 20.600 67.800 1.00 53.19 B O ATOM 2159 N MET B 94 −2.463 20.112 69.438 1.00 54.33 B N ATOM 2160 CA MET B 94 −1.475 20.105 70.518 1.00 54.32 B C ATOM 2161 CB MET B 94 −2.187 20.187 71.865 1.00 54.57 B C ATOM 2162 CG MET B 94 −2.912 21.495 72.085 1.00 55.46 B C ATOM 2163 SD MET B 94 −4.430 21.279 73.060 1.00 59.01 B S ATOM 2164 CE MET B 94 −4.108 22.396 74.457 1.00 57.26 B C ATOM 2165 C MET B 94 −0.593 18.865 70.478 1.00 54.68 B C ATOM 2166 O MET B 94 0.525 18.860 71.001 1.00 55.26 B O ATOM 2167 N ARG B 95 −1.111 17.818 69.849 1.00 54.49 B N ATOM 2168 CA ARG B 95 −0.433 16.528 69.765 1.00 53.38 B C ATOM 2169 CB ARG B 95 −1.432 15.462 69.302 1.00 55.43 B C ATOM 2170 CG ARG B 95 −1.275 14.112 69.962 1.00 56.55 B C ATOM 2171 CD ARG B 95 −2.620 13.441 70.086 1.00 59.84 B C ATOM 2172 NE ARG B 95 −3.233 13.690 71.391 1.00 64.42 B N ATOM 2173 CZ ARG B 95 −4.533 13.562 71.646 1.00 65.28 B C ATOM 2174 NH1 ARG B 95 −5.361 13.190 70.677 1.00 65.14 B N ATOM 2175 NH2 ARG B 95 −5.004 13.792 72.868 1.00 65.12 B N ATOM 2176 C ARG B 95 0.717 16.627 68.775 1.00 51.01 B C ATOM 2177 O ARG B 95 1.780 16.051 68.987 1.00 51.64 B O ATOM 2178 N THR B 96 0.492 17.376 67.701 1.00 48.27 B N ATOM 2179 CA THR B 96 1.465 17.522 66.634 1.00 46.45 B C ATOM 2180 CB THR B 96 0.725 18.021 65.331 1.00 47.46 B C ATOM 2181 OG1 THR B 96 1.669 18.531 64.381 1.00 50.40 B O ATOM 2182 CG2 THR B 96 −0.311 19.079 65.659 1.00 47.39 B C ATOM 2183 C THR B 96 2.686 18.406 66.986 1.00 44.27 B C ATOM 2184 O THR B 96 2.569 19.427 67.662 1.00 40.44 B O ATOM 2185 N PRO B 97 3.884 17.981 66.544 1.00 43.87 B N ATOM 2186 CD PRO B 97 4.038 16.669 65.894 1.00 42.64 B C ATOM 2187 CA PRO B 97 5.174 18.679 66.675 1.00 43.84 B C ATOM 2188 CB PRO B 97 6.137 17.815 65.873 1.00 43.21 B C ATOM 2189 CG PRO B 97 5.517 16.457 65.916 1.00 44.59 B C ATOM 2190 C PRO B 97 5.144 20.099 66.138 1.00 44.58 B C ATOM 2191 O PRO B 97 4.557 20.359 65.097 1.00 46.08 B O ATOM 2192 N ARG B 98 5.787 21.018 66.843 1.00 42.67 B N ATOM 2193 CA ARG B 98 5.762 22.407 66.438 1.00 41.79 B C ATOM 2194 CB ARG B 98 4.597 23.115 67.080 1.00 39.57 B C ATOM 2195 CG ARG B 98 4.658 23.024 68.585 1.00 38.84 B C ATOM 2196 CD ARG B 98 3.626 23.918 69.214 1.00 36.53 B C ATOM 2197 NE ARG B 98 4.069 25.297 69.136 1.00 37.53 B N ATOM 2198 CZ ARG B 98 3.326 26.340 69.468 1.00 38.37 B C ATOM 2199 NH1 ARG B 98 2.092 26.166 69.904 1.00 41.50 B N ATOM 2200 NH2 ARG B 98 3.824 27.558 69.369 1.00 38.22 B N ATOM 2201 C ARG B 98 7.034 23.102 66.858 1.00 42.54 B C ATOM 2202 O ARG B 98 8.035 22.462 67.193 1.00 43.92 B O ATOM 2203 N CYS B 99 6.977 24.427 66.850 1.00 40.74 B N ATOM 2204 CA CYS B 99 8.104 25.267 67.216 1.00 39.39 B C ATOM 2205 CB CYS B 99 8.134 26.466 66.263 1.00 34.48 B C ATOM 2206 SG CYS B 99 9.125 27.822 66.800 1.00 30.47 B S ATOM 2207 C CYS B 99 8.004 25.720 68.693 1.00 41.89 B C ATOM 2208 O CYS B 99 6.902 25.912 69.227 1.00 42.28 B O ATOM 2209 N GLY B 100 9.152 25.881 69.350 1.00 41.35 B N ATOM 2210 CA GLY B 100 9.154 26.116 70.785 1.00 41.80 B C ATOM 2211 C GLY B 100 8.884 27.560 71.137 1.00 41.15 B C ATOM 2212 O GLY B 100 8.399 27.889 72.211 1.00 42.29 B O ATOM 2213 N VAL B 101 9.193 28.444 70.218 1.00 40.80 B N ATOM 2214 CA VAL B 101 8.910 29.842 70.444 1.00 41.25 B C ATOM 2215 CB VAL B 101 9.397 30.645 69.242 1.00 40.41 B C ATOM 2216 CG1 VAL B 101 8.802 32.037 69.273 1.00 40.34 B C ATOM 2217 CG2 VAL B 101 10.941 30.708 69.269 1.00 39.99 B C ATOM 2218 C VAL B 101 7.428 30.153 70.721 1.00 41.68 B C ATOM 2219 O VAL B 101 6.537 29.692 70.021 1.00 43.24 B O ATOM 2220 N PRO B 102 7.146 30.958 71.747 1.00 40.72 B N ATOM 2221 CD PRO B 102 8.053 31.428 72.806 1.00 39.17 B C ATOM 2222 CA PRO B 102 5.733 31.226 72.061 1.00 39.57 B C ATOM 2223 CB PRO B 102 5.799 31.977 73.392 1.00 39.49 B C ATOM 2224 CG PRO B 102 7.129 31.569 73.987 1.00 39.01 B C ATOM 2225 C PRO B 102 4.968 32.010 70.988 1.00 36.64 B C ATOM 2226 O PRO B 102 3.737 32.133 71.049 1.00 35.95 B O ATOM 2227 N THR B 109 11.901 38.959 77.442 1.00 55.11 B N ATOM 2228 CA THR B 109 12.364 40.350 77.502 1.00 55.36 B C ATOM 2229 CB THR B 109 12.645 40.798 78.940 1.00 56.98 B C ATOM 2230 OG1 THR B 109 11.408 40.938 79.664 1.00 56.86 B O ATOM 2231 CG2 THR B 109 13.405 42.124 78.923 1.00 57.52 B C ATOM 2232 C THR B 109 13.638 40.580 76.714 1.00 54.54 B C ATOM 2233 O THR B 109 14.687 40.031 77.044 1.00 54.74 B O ATOM 2234 N PHE B 110 13.552 41.420 75.691 1.00 53.48 B N ATOM 2235 CA PHE B 110 14.602 41.495 74.679 1.00 51.99 B C ATOM 2236 CB PHE B 110 14.096 40.918 73.362 1.00 48.67 B C ATOM 2237 CG PHE B 110 14.026 39.453 73.351 1.00 46.48 B C ATOM 2238 CD1 PHE B 110 12.819 38.816 73.194 1.00 47.06 B C ATOM 2239 CD2 PHE B 110 15.177 38.704 73.503 1.00 46.90 B C ATOM 2240 CE1 PHE B 110 12.757 37.444 73.187 1.00 48.71 B C ATOM 2241 CE2 PHE B 110 15.129 37.335 73.498 1.00 48.40 B C ATOM 2242 CZ PHE B 110 13.918 36.695 73.340 1.00 48.41 B C ATOM 2243 C PHE B 110 15.103 42.897 74.421 1.00 52.26 B C ATOM 2244 O PHE B 110 14.465 43.875 74.791 1.00 52.08 B O ATOM 2245 N GLU B 111 16.244 42.984 73.756 1.00 53.92 B N ATOM 2246 CA GLU B 111 16.878 44.268 73.512 1.00 55.45 B C ATOM 2247 CB GLU B 111 18.330 44.190 73.972 1.00 57.42 B C ATOM 2248 CG GLU B 111 18.977 45.521 74.243 1.00 60.30 B C ATOM 2249 CD GLU B 111 20.374 45.362 74.804 1.00 62.77 B C ATOM 2250 OE1 GLU B 111 20.674 44.242 75.293 1.00 63.66 B O ATOM 2251 OE2 GLU B 111 21.166 46.345 74.756 1.00 62.77 B O ATOM 2252 C GLU B 111 16.804 44.720 72.039 1.00 55.15 B C ATOM 2253 O GLU B 111 17.178 43.980 71.122 1.00 56.14 B O ATOM 2254 N GLY B 112 16.300 45.937 71.832 1.00 55.02 B N ATOM 2255 CA GLY B 112 16.349 46.568 70.523 1.00 52.56 B C ATOM 2256 C GLY B 112 15.042 46.656 69.744 1.00 51.35 B C ATOM 2257 O GLY B 112 13.982 46.285 70.237 1.00 50.10 B O ATOM 2258 N ASP B 113 15.138 47.165 68.517 1.00 51.06 B N ATOM 2259 CA ASP B 113 14.068 47.105 67.533 1.00 50.58 B C ATOM 2260 CB ASP B 113 14.523 47.776 66.243 1.00 53.82 B C ATOM 2261 CG ASP B 113 14.107 49.203 66.180 1.00 58.14 B C ATOM 2262 OD1 ASP B 113 13.707 49.721 67.249 1.00 61.51 B O ATOM 2263 OD2 ASP B 113 14.167 49.805 65.084 1.00 59.88 B O ATOM 2264 C ASP B 113 13.579 45.703 67.187 1.00 48.96 B C ATOM 2265 O ASP B 113 12.497 45.545 66.610 1.00 46.57 B O ATOM 2266 N LEU B 114 14.386 44.699 67.510 1.00 48.26 B N ATOM 2267 CA LEU B 114 14.121 43.342 67.072 1.00 49.73 B C ATOM 2268 CB LEU B 114 12.821 42.813 67.702 1.00 49.40 B C ATOM 2269 CG LEU B 114 12.626 42.973 69.218 1.00 47.95 B C ATOM 2270 CD1 LEU B 114 11.433 42.157 69.698 1.00 45.23 B C ATOM 2271 CD2 LEU B 114 13.881 42.517 69.913 1.00 47.54 B C ATOM 2272 C LEU B 114 14.017 43.277 65.537 1.00 50.53 B C ATOM 2273 O LEU B 114 13.256 42.463 64.992 1.00 52.04 B O ATOM 2274 N LYS B 115 14.752 44.168 64.861 1.00 51.89 B N ATOM 2275 CA LYS B 115 15.076 44.076 63.431 1.00 49.99 B C ATOM 2276 CB LYS B 115 14.399 45.186 62.607 1.00 51.78 B C ATOM 2277 CG LYS B 115 12.901 45.018 62.360 1.00 52.75 B C ATOM 2278 CD LYS B 115 12.336 46.045 61.343 1.00 52.50 B C ATOM 2279 CE LYS B 115 12.725 47.494 61.646 1.00 49.79 B C ATOM 2280 NZ LYS B 115 14.069 47.806 61.114 1.00 47.18 B N ATOM 2281 C LYS B 115 16.587 44.231 63.259 1.00 49.76 B C ATOM 2282 O LYS B 115 17.306 44.552 64.204 1.00 49.70 B O ATOM 2283 N TRP B 116 17.063 44.027 62.037 1.00 49.31 B N ATOM 2284 CA TRP B 116 18.464 44.226 61.742 1.00 47.10 B C ATOM 2285 CB TRP B 116 18.895 43.219 60.708 1.00 45.52 B C ATOM 2286 CG TRP B 116 18.903 41.842 61.269 1.00 45.03 B C ATOM 2287 CD2 TRP B 116 19.886 41.288 62.142 1.00 43.32 B C ATOM 2288 CE2 TRP B 116 19.517 39.946 62.385 1.00 44.57 B C ATOM 2289 CE3 TRP B 116 21.039 41.795 62.740 1.00 40.58 B C ATOM 2290 CD1 TRP B 116 17.994 40.846 61.027 1.00 45.95 B C ATOM 2291 NE1 TRP B 116 18.358 39.702 61.693 1.00 45.13 B N ATOM 2292 CZ2 TRP B 116 20.271 39.103 63.202 1.00 43.39 B C ATOM 2293 CZ3 TRP B 116 21.780 40.972 63.544 1.00 41.21 B C ATOM 2294 CH2 TRP B 116 21.395 39.629 63.772 1.00 42.59 B C ATOM 2295 C TRP B 116 18.717 45.630 61.264 1.00 47.50 B C ATOM 2296 O TRP B 116 17.860 46.251 60.631 1.00 48.31 B O ATOM 2297 N HIS B 117 19.893 46.158 61.565 1.00 48.67 B N ATOM 2298 CA HIS B 117 20.149 47.527 61.156 1.00 49.40 B C ATOM 2299 CB HIS B 117 20.297 48.407 62.397 1.00 50.74 B C ATOM 2300 CG HIS B 117 19.004 48.620 63.132 1.00 51.22 B C ATOM 2301 CD2 HIS B 117 17.884 49.306 62.792 1.00 51.17 B C ATOM 2302 ND1 HIS B 117 18.755 48.080 64.377 1.00 51.48 B N ATOM 2303 CE1 HIS B 117 17.541 48.425 64.773 1.00 51.43 B C ATOM 2304 NE2 HIS B 117 16.991 49.170 63.830 1.00 51.55 B N ATOM 2305 C HIS B 117 21.335 47.665 60.205 1.00 48.49 B C ATOM 2306 O HIS B 117 21.782 48.778 59.907 1.00 48.60 B O ATOM 2307 N HIS B 118 21.821 46.520 59.718 1.00 48.21 B N ATOM 2308 CA HIS B 118 22.772 46.477 58.608 1.00 46.67 B C ATOM 2309 CB HIS B 118 24.161 46.088 59.104 1.00 46.05 B C ATOM 2310 CG HIS B 118 24.166 44.915 60.025 1.00 47.16 B C ATOM 2311 CD2 HIS B 118 24.582 43.639 59.844 1.00 48.01 B C ATOM 2312 ND1 HIS B 118 23.663 44.977 61.307 1.00 47.95 B N ATOM 2313 CE1 HIS B 118 23.765 43.789 61.876 1.00 49.06 B C ATOM 2314 NE2 HIS B 118 24.319 42.959 61.010 1.00 49.48 B N ATOM 2315 C HIS B 118 22.310 45.505 57.527 1.00 46.51 B C ATOM 2316 O HIS B 118 21.168 45.059 57.525 1.00 45.67 B O ATOM 2317 N HIS B 119 23.179 45.192 56.583 1.00 47.29 B N ATOM 2318 CA HIS B 119 22.682 44.564 55.383 1.00 48.75 B C ATOM 2319 CB HIS B 119 23.019 45.420 54.153 1.00 53.33 B C ATOM 2320 CG HIS B 119 22.176 46.653 54.035 1.00 57.38 B C ATOM 2321 CD2 HIS B 119 20.833 46.807 53.948 1.00 58.70 B C ATOM 2322 ND1 HIS B 119 22.708 47.927 54.025 1.00 59.87 B N ATOM 2323 CE1 HIS B 119 21.729 48.812 53.938 1.00 60.33 B C ATOM 2324 NE2 HIS B 119 20.581 48.158 53.891 1.00 60.33 B N ATOM 2325 C HIS B 119 23.195 43.158 55.215 1.00 47.70 B C ATOM 2326 O HIS B 119 22.442 42.261 54.841 1.00 47.36 B O ATOM 2327 N ASN B 120 24.476 42.959 55.495 1.00 47.99 B N ATOM 2328 CA ASN B 120 25.040 41.622 55.409 1.00 47.22 B C ATOM 2329 CB ASN B 120 26.483 41.664 54.911 1.00 48.97 B C ATOM 2330 CG ASN B 120 27.006 40.278 54.540 1.00 52.10 B C ATOM 2331 OD1 ASN B 120 26.227 39.386 54.163 1.00 53.12 B O ATOM 2332 ND2 ASN B 120 28.327 40.085 54.650 1.00 52.17 B N ATOM 2333 C ASN B 120 24.978 40.955 56.775 1.00 45.83 B C ATOM 2334 O ASN B 120 25.594 41.418 57.746 1.00 45.09 B O ATOM 2335 N ILE B 121 24.214 39.869 56.839 1.00 42.91 B N ATOM 2336 CA ILE B 121 24.043 39.138 58.075 1.00 41.02 B C ATOM 2337 CB ILE B 121 22.594 38.725 58.266 1.00 39.38 B C ATOM 2338 CG2 ILE B 121 22.413 38.098 59.615 1.00 38.99 B C ATOM 2339 CG1 ILE B 121 21.711 39.963 58.225 1.00 40.20 B C ATOM 2340 CD1 ILE B 121 22.095 40.977 59.271 1.00 39.34 B C ATOM 2341 C ILE B 121 24.940 37.927 58.014 1.00 40.88 B C ATOM 2342 O ILE B 121 24.981 37.237 56.999 1.00 40.80 B O ATOM 2343 N THR B 122 25.696 37.694 59.082 1.00 41.16 B N ATOM 2344 CA THR B 122 26.764 36.693 59.044 1.00 41.23 B C ATOM 2345 CB THR B 122 28.092 37.257 59.478 1.00 41.88 B C ATOM 2346 OG1 THR B 122 27.958 37.723 60.823 1.00 42.35 B O ATOM 2347 CG2 THR B 122 28.523 38.403 58.577 1.00 41.22 B C ATOM 2348 C THR B 122 26.482 35.590 60.015 1.00 39.79 B C ATOM 2349 O THR B 122 26.373 35.840 61.209 1.00 41.25 B O ATOM 2350 N TYR B 123 26.415 34.368 59.499 1.00 40.55 B N ATOM 2351 CA TYR B 123 26.026 33.218 60.296 1.00 39.60 B C ATOM 2352 CB TYR B 123 24.798 32.568 59.681 1.00 37.77 B C ATOM 2353 CG TYR B 123 25.057 31.795 58.409 1.00 37.99 B C ATOM 2354 CD1 TYR B 123 25.115 32.438 57.166 1.00 36.75 B C ATOM 2355 CE1 TYR B 123 25.226 31.708 55.993 1.00 36.06 B C ATOM 2356 CD2 TYR B 123 25.136 30.403 58.434 1.00 37.82 B C ATOM 2357 CE2 TYR B 123 25.251 29.669 57.274 1.00 36.30 B C ATOM 2358 CZ TYR B 123 25.288 30.316 56.061 1.00 37.33 B C ATOM 2359 OH TYR B 123 25.340 29.545 54.920 1.00 38.75 B O ATOM 2360 C TYR B 123 27.143 32.181 60.460 1.00 41.07 B C ATOM 2361 O TYR B 123 27.939 31.953 59.540 1.00 39.95 B O ATOM 2362 N TRP B 124 27.176 31.574 61.651 1.00 40.96 B N ATOM 2363 CA TRP B 124 28.124 30.537 62.033 1.00 41.66 B C ATOM 2364 CB TRP B 124 28.906 30.982 63.272 1.00 43.80 B C ATOM 2365 CG TRP B 124 29.970 30.003 63.712 1.00 45.96 B C ATOM 2366 CD2 TRP B 124 30.468 29.813 65.046 1.00 46.71 B C ATOM 2367 CE2 TRP B 124 31.474 28.815 64.979 1.00 45.97 B C ATOM 2368 CE3 TRP B 124 30.169 30.390 66.290 1.00 48.17 B C ATOM 2369 CD1 TRP B 124 30.679 29.131 62.911 1.00 45.99 B C ATOM 2370 NE1 TRP B 124 31.579 28.419 63.670 1.00 45.74 B N ATOM 2371 CZ2 TRP B 124 32.178 28.380 66.107 1.00 45.22 B C ATOM 2372 CZ3 TRP B 124 30.879 29.951 67.422 1.00 48.24 B C ATOM 2373 CH2 TRP B 124 31.872 28.954 67.313 1.00 46.12 B C ATOM 2374 C TRP B 124 27.409 29.220 62.343 1.00 42.06 B C ATOM 2375 O TRP B 124 26.587 29.154 63.258 1.00 43.39 B O ATOM 2376 N ILE B 125 27.721 28.185 61.569 1.00 41.65 B N ATOM 2377 CA ILE B 125 27.308 26.816 61.871 1.00 42.68 B C ATOM 2378 CB ILE B 125 27.356 25.931 60.603 1.00 43.36 B C ATOM 2379 CG2 ILE B 125 27.028 24.485 60.949 1.00 43.97 B C ATOM 2380 CG1 ILE B 125 26.401 26.479 59.545 1.00 43.65 B C ATOM 2381 CD1 ILE B 125 26.622 25.861 58.181 1.00 41.39 B C ATOM 2382 C ILE B 125 28.311 26.252 62.865 1.00 41.25 B C ATOM 2383 O ILE B 125 29.417 25.886 62.477 1.00 42.48 B O ATOM 2384 N GLN B 126 27.929 26.176 64.139 1.00 42.10 B N ATOM 2385 CA GLN B 126 28.896 25.922 65.205 1.00 40.20 B C ATOM 2386 CB GLN B 126 28.621 26.828 66.397 1.00 42.38 B C ATOM 2387 CG GLN B 126 27.681 26.225 67.407 1.00 50.00 B C ATOM 2388 CD GLN B 126 27.621 27.031 68.705 1.00 54.69 B C ATOM 2389 OE1 GLN B 126 26.561 27.140 69.360 1.00 56.32 B O ATOM 2390 NE2 GLN B 126 28.767 27.604 69.086 1.00 58.22 B N ATOM 2391 C GLN B 126 28.992 24.480 65.690 1.00 37.48 B C ATOM 2392 O GLN B 126 29.901 24.147 66.436 1.00 37.51 B O ATOM 2393 N ASN B 127 28.079 23.616 65.276 0.50 38.49 B N ATOM 2394 CA ASN B 127 28.297 22.193 65.480 0.50 38.69 B C ATOM 2395 CB ASN B 127 28.032 21.790 66.928 0.50 37.72 B C ATOM 2396 CG ASN B 127 26.736 22.337 67.446 0.50 37.87 B C ATOM 2397 OD1 ASN B 127 26.115 23.192 66.815 0.50 39.08 B O ATOM 2398 ND2 ASN B 127 26.315 21.858 68.602 0.50 36.28 B N ATOM 2399 C ASN B 127 27.397 21.426 64.550 0.50 40.83 B C ATOM 2400 O ASN B 127 26.567 22.021 63.874 0.50 41.26 B O ATOM 2401 N TYR B 128 27.565 20.108 64.507 1.00 43.09 B N ATOM 2402 CA TYR B 128 26.925 19.295 63.478 1.00 43.60 B C ATOM 2403 CB TYR B 128 27.962 18.825 62.466 1.00 45.04 B C ATOM 2404 CG TYR B 128 28.287 19.841 61.391 1.00 47.51 B C ATOM 2405 CD1 TYR B 128 27.538 19.905 60.215 1.00 48.05 B C ATOM 2406 CE1 TYR B 128 27.866 20.800 59.199 1.00 48.73 B C ATOM 2407 CD2 TYR B 128 29.373 20.707 61.528 1.00 47.75 B C ATOM 2408 CE2 TYR B 128 29.709 21.604 60.524 1.00 47.49 B C ATOM 2409 CZ TYR B 128 28.954 21.645 59.358 1.00 48.46 B C ATOM 2410 OH TYR B 128 29.302 22.512 58.346 1.00 45.74 B O ATOM 2411 C TYR B 128 26.162 18.082 63.985 1.00 44.90 B C ATOM 2412 O TYR B 128 26.713 17.211 64.664 1.00 46.03 B O ATOM 2413 N SER B 129 24.890 18.001 63.624 1.00 45.04 B N ATOM 2414 CA SER B 129 24.155 16.768 63.859 1.00 45.77 B C ATOM 2415 CB SER B 129 22.674 16.953 63.543 1.00 43.66 B C ATOM 2416 OG SER B 129 22.025 15.702 63.584 1.00 41.28 B O ATOM 2417 C SER B 129 24.727 15.646 62.994 1.00 47.15 B C ATOM 2418 O SER B 129 25.471 15.883 62.041 1.00 47.19 B O ATOM 2419 N GLU B 130 24.371 14.415 63.320 1.00 49.17 B N ATOM 2420 CA GLU B 130 25.013 13.284 62.676 1.00 51.22 B C ATOM 2421 CB GLU B 130 25.649 12.380 63.734 1.00 53.34 B C ATOM 2422 CG GLU B 130 26.603 13.112 64.677 1.00 57.56 B C ATOM 2423 CD GLU B 130 28.058 12.690 64.510 1.00 60.18 B C ATOM 2424 OE1 GLU B 130 28.325 11.467 64.547 1.00 62.12 B O ATOM 2425 OE2 GLU B 130 28.937 13.582 64.348 1.00 61.07 B O ATOM 2426 C GLU B 130 24.074 12.475 61.795 1.00 50.78 B C ATOM 2427 O GLU B 130 24.471 11.444 61.258 1.00 50.80 B O ATOM 2428 N ASP B 131 22.834 12.940 61.643 1.00 51.25 B N ATOM 2429 CA ASP B 131 21.857 12.245 60.793 1.00 50.61 B C ATOM 2430 CB ASP B 131 20.439 12.644 61.187 1.00 50.45 B C ATOM 2431 CG ASP B 131 20.181 12.454 62.666 1.00 51.11 B C ATOM 2432 OD1 ASP B 131 20.983 11.731 63.312 1.00 51.11 B O ATOM 2433 OD2 ASP B 131 19.184 13.026 63.174 1.00 48.43 B O ATOM 2434 C ASP B 131 22.085 12.536 59.313 1.00 51.33 B C ATOM 2435 O ASP B 131 21.681 11.754 58.444 1.00 51.91 B O ATOM 2436 N LEU B 132 22.736 13.667 59.044 1.00 49.15 B N ATOM 2437 CA LEU B 132 23.142 14.041 57.700 1.00 46.80 B C ATOM 2438 CB LEU B 132 22.478 15.363 57.317 1.00 45.75 B C ATOM 2439 CG LEU B 132 20.949 15.419 57.303 1.00 43.95 B C ATOM 2440 CD1 LEU B 132 20.505 16.844 57.096 1.00 43.72 B C ATOM 2441 CD2 LEU B 132 20.407 14.557 56.180 1.00 44.26 B C ATOM 2442 C LEU B 132 24.665 14.187 57.632 1.00 46.69 B C ATOM 2443 O LEU B 132 25.318 14.447 58.640 1.00 47.59 B O ATOM 2444 N PRO B 133 25.251 14.007 56.437 1.00 46.39 B N ATOM 2445 CD PRO B 133 24.677 13.251 55.310 1.00 46.66 B C ATOM 2446 CA PRO B 133 26.642 14.402 56.176 1.00 46.99 B C ATOM 2447 CB PRO B 133 26.891 13.923 54.747 1.00 45.70 B C ATOM 2448 CG PRO B 133 25.892 12.823 54.539 1.00 45.43 B C ATOM 2449 C PRO B 133 26.803 15.915 56.303 1.00 47.78 B C ATOM 2450 O PRO B 133 25.861 16.666 56.022 1.00 47.82 B O ATOM 2451 N ARG B 134 27.993 16.360 56.717 1.00 49.83 B N ATOM 2452 CA ARG B 134 28.256 17.789 56.990 1.00 49.68 B C ATOM 2453 CB ARG B 134 29.678 17.987 57.528 1.00 51.29 B C ATOM 2454 CG ARG B 134 29.847 17.752 59.007 1.00 53.28 B C ATOM 2455 CD ARG B 134 31.135 18.400 59.511 1.00 54.49 B C ATOM 2456 NE ARG B 134 31.377 18.104 60.919 1.00 55.78 B N ATOM 2457 CZ ARG B 134 32.244 18.751 61.689 1.00 56.23 B C ATOM 2458 NH1 ARG B 134 32.965 19.747 61.183 1.00 55.60 B N ATOM 2459 NH2 ARG B 134 32.382 18.404 62.968 1.00 57.18 B N ATOM 2460 C ARG B 134 28.072 18.738 55.801 1.00 47.81 B C ATOM 2461 O ARG B 134 27.721 19.909 55.987 1.00 47.97 B O ATOM 2462 N ALA B 135 28.339 18.241 54.594 1.00 45.58 B N ATOM 2463 CA ALA B 135 28.066 19.001 53.376 1.00 43.47 B C ATOM 2464 CB ALA B 135 28.692 18.306 52.175 1.00 41.20 B C ATOM 2465 C ALA B 135 26.554 19.162 53.163 1.00 42.31 B C ATOM 2466 O ALA B 135 26.078 20.250 52.846 1.00 41.35 B O ATOM 2467 N VAL B 136 25.806 18.080 53.347 1.00 40.97 B N ATOM 2468 CA VAL B 136 24.359 18.140 53.233 1.00 40.01 B C ATOM 2469 CB VAL B 136 23.724 16.771 53.518 1.00 39.78 B C ATOM 2470 CG1 VAL B 136 22.241 16.920 53.732 1.00 40.96 B C ATOM 2471 CG2 VAL B 136 23.987 15.841 52.361 1.00 38.01 B C ATOM 2472 C VAL B 136 23.735 19.176 54.169 1.00 41.05 B C ATOM 2473 O VAL B 136 22.717 19.784 53.832 1.00 40.50 B O ATOM 2474 N ILE B 137 24.353 19.382 55.331 1.00 40.89 B N ATOM 2475 CA ILE B 137 23.826 20.294 56.349 1.00 41.02 B C ATOM 2476 CB ILE B 137 24.449 19.984 57.752 1.00 40.35 B C ATOM 2477 CG2 ILE B 137 24.170 21.111 58.731 1.00 41.40 B C ATOM 2478 CG1 ILE B 137 23.889 18.653 58.288 1.00 40.52 B C ATOM 2479 CD1 ILE B 137 24.456 18.215 59.633 1.00 37.58 B C ATOM 2480 C ILE B 137 24.076 21.750 55.957 1.00 41.91 B C ATOM 2481 O ILE B 137 23.139 22.560 55.856 1.00 41.25 B O ATOM 2482 N ASP B 138 25.335 22.083 55.707 1.00 43.24 B N ATOM 2483 CA ASP B 138 25.661 23.413 55.207 1.00 44.74 B C ATOM 2484 CB ASP B 138 27.081 23.431 54.632 1.00 46.86 B C ATOM 2485 CG ASP B 138 28.139 23.229 55.695 1.00 51.02 B C ATOM 2486 OD1 ASP B 138 28.783 22.145 55.717 1.00 53.15 B O ATOM 2487 OD2 ASP B 138 28.326 24.162 56.515 1.00 53.20 B O ATOM 2488 C ASP B 138 24.666 23.811 54.133 1.00 43.68 B C ATOM 2489 O ASP B 138 24.167 24.932 54.115 1.00 44.60 B O ATOM 2490 N ASP B 139 24.373 22.870 53.245 1.00 43.96 B N ATOM 2491 CA ASP B 139 23.570 23.162 52.075 1.00 42.60 B C ATOM 2492 CB ASP B 139 23.605 21.991 51.104 1.00 43.34 B C ATOM 2493 CG ASP B 139 22.905 22.304 49.796 1.00 45.53 B C ATOM 2494 OD1 ASP B 139 23.533 22.958 48.928 1.00 47.55 B O ATOM 2495 OD2 ASP B 139 21.727 21.902 49.624 1.00 47.31 B O ATOM 2496 C ASP B 139 22.137 23.444 52.476 1.00 42.21 B C ATOM 2497 O ASP B 139 21.474 24.312 51.899 1.00 41.13 B O ATOM 2498 N ALA B 140 21.638 22.707 53.455 1.00 41.74 B N ATOM 2499 CA ALA B 140 20.251 22.911 53.814 1.00 43.53 B C ATOM 2500 CB ALA B 140 19.774 21.844 54.800 1.00 42.75 B C ATOM 2501 C ALA B 140 20.154 24.302 54.427 1.00 43.95 B C ATOM 2502 O ALA B 140 19.243 25.067 54.105 1.00 43.98 B O ATOM 2503 N PHE B 141 21.116 24.642 55.281 1.00 43.60 B N ATOM 2504 CA PHE B 141 21.097 25.952 55.908 1.00 42.93 B C ATOM 2505 CB PHE B 141 22.229 26.088 56.940 1.00 42.04 B C ATOM 2506 CG PHE B 141 21.943 25.377 58.239 1.00 40.59 B C ATOM 2507 CD1 PHE B 141 20.633 25.118 58.620 1.00 38.33 B C ATOM 2508 CD2 PHE B 141 22.972 24.926 59.048 1.00 39.63 B C ATOM 2509 CE1 PHE B 141 20.353 24.422 59.768 1.00 36.71 B C ATOM 2510 CE2 PHE B 141 22.700 24.226 60.205 1.00 38.82 B C ATOM 2511 CZ PHE B 141 21.385 23.974 60.561 1.00 37.71 B C ATOM 2512 C PHE B 141 21.169 27.081 54.881 1.00 43.11 B C ATOM 2513 O PHE B 141 20.305 27.968 54.878 1.00 45.28 B O ATOM 2514 N ALA B 142 22.165 27.052 53.998 1.00 40.49 B N ATOM 2515 CA ALA B 142 22.291 28.095 52.978 1.00 37.84 B C ATOM 2516 CB ALA B 142 23.506 27.826 52.118 1.00 36.79 B C ATOM 2517 C ALA B 142 21.042 28.192 52.104 1.00 37.51 B C ATOM 2518 O ALA B 142 20.496 29.278 51.894 1.00 33.84 B O ATOM 2519 N ARG B 143 20.594 27.043 51.609 1.00 39.12 B N ATOM 2520 CA ARG B 143 19.342 26.941 50.867 1.00 41.61 B C ATOM 2521 CB ARG B 143 18.945 25.480 50.719 1.00 42.92 B C ATOM 2522 CG ARG B 143 19.025 24.996 49.296 1.00 43.85 B C ATOM 2523 CD ARG B 143 19.110 23.488 49.216 1.00 43.74 B C ATOM 2524 NE ARG B 143 17.872 22.828 49.588 1.00 43.94 B N ATOM 2525 CZ ARG B 143 17.839 21.799 50.418 1.00 43.07 B C ATOM 2526 NH1 ARG B 143 18.975 21.359 50.933 1.00 44.72 B N ATOM 2527 NH2 ARG B 143 16.693 21.201 50.722 1.00 45.28 B N ATOM 2528 C ARG B 143 18.209 27.681 51.548 1.00 42.45 B C ATOM 2529 O ARG B 143 17.360 28.288 50.902 1.00 44.06 B O ATOM 2530 N ALA B 144 18.194 27.606 52.869 1.00 41.78 B N ATOM 2531 CA ALA B 144 17.174 28.269 53.642 1.00 39.35 B C ATOM 2532 CB ALA B 144 17.194 27.756 55.055 1.00 38.33 B C ATOM 2533 C ALA B 144 17.392 29.778 53.613 1.00 39.06 B C ATOM 2534 O ALA B 144 16.445 30.545 53.416 1.00 40.22 B O ATOM 2535 N PHE B 145 18.629 30.218 53.803 1.00 38.92 B N ATOM 2536 CA PHE B 145 18.899 31.645 53.717 1.00 38.87 B C ATOM 2537 CB PHE B 145 20.370 31.944 54.065 1.00 35.84 B C ATOM 2538 CG PHE B 145 20.636 32.010 55.545 1.00 35.24 B C ATOM 2539 CD1 PHE B 145 19.991 32.956 56.334 1.00 34.91 B C ATOM 2540 CD2 PHE B 145 21.497 31.109 56.161 1.00 35.25 B C ATOM 2541 CE1 PHE B 145 20.193 33.004 57.713 1.00 33.99 B C ATOM 2542 CE2 PHE B 145 21.709 31.147 57.550 1.00 34.41 B C ATOM 2543 CZ PHE B 145 21.054 32.098 58.326 1.00 34.36 B C ATOM 2544 C PHE B 145 18.544 32.158 52.314 1.00 39.05 B C ATOM 2545 O PHE B 145 18.129 33.312 52.141 1.00 38.80 B O ATOM 2546 N ALA B 146 18.669 31.290 51.313 1.00 39.50 B N ATOM 2547 CA ALA B 146 18.423 31.722 49.943 1.00 39.75 B C ATOM 2548 CB ALA B 146 18.784 30.621 48.958 1.00 39.43 B C ATOM 2549 C ALA B 146 16.960 32.128 49.777 1.00 41.33 B C ATOM 2550 O ALA B 146 16.659 33.076 49.048 1.00 42.06 B O ATOM 2551 N LEU B 147 16.053 31.437 50.467 1.00 39.32 B N ATOM 2552 CA LEU B 147 14.652 31.848 50.455 1.00 39.31 B C ATOM 2553 CB LEU B 147 13.828 31.069 51.490 1.00 38.14 B C ATOM 2554 CG LEU B 147 13.308 29.668 51.134 1.00 37.99 B C ATOM 2555 CD1 LEU B 147 12.598 29.101 52.332 1.00 36.24 B C ATOM 2556 CD2 LEU B 147 12.366 29.718 49.943 1.00 35.55 B C ATOM 2557 C LEU B 147 14.568 33.332 50.773 1.00 39.71 B C ATOM 2558 O LEU B 147 14.128 34.133 49.946 1.00 41.25 B O ATOM 2559 N TRP B 148 15.025 33.702 51.966 1.00 40.57 B N ATOM 2560 CA TRP B 148 14.739 35.024 52.514 1.00 39.24 B C ATOM 2561 CB TRP B 148 15.092 35.062 54.013 1.00 37.40 B C ATOM 2562 CG TRP B 148 14.107 34.282 54.858 1.00 35.82 B C ATOM 2563 CD2 TRP B 148 12.705 34.558 55.040 1.00 35.94 B C ATOM 2564 CE2 TRP B 148 12.160 33.496 55.794 1.00 35.14 B C ATOM 2565 CE3 TRP B 148 11.856 35.593 54.634 1.00 36.07 B C ATOM 2566 CD1 TRP B 148 14.342 33.103 55.507 1.00 36.48 B C ATOM 2567 NE1 TRP B 148 13.179 32.622 56.067 1.00 34.94 B N ATOM 2568 CZ2 TRP B 148 10.807 33.442 56.146 1.00 34.07 B C ATOM 2569 CZ3 TRP B 148 10.505 35.532 54.990 1.00 34.15 B C ATOM 2570 CH2 TRP B 148 10.001 34.465 55.735 1.00 32.87 B C ATOM 2571 C TRP B 148 15.472 36.102 51.741 1.00 38.45 B C ATOM 2572 O TRP B 148 15.024 37.247 51.651 1.00 37.45 B O ATOM 2573 N SER B 149 16.593 35.719 51.153 1.00 40.24 B N ATOM 2574 CA SER B 149 17.411 36.683 50.423 1.00 41.85 B C ATOM 2575 CB SER B 149 18.724 36.031 49.987 1.00 41.87 B C ATOM 2576 OG SER B 149 19.580 36.991 49.410 1.00 41.32 B O ATOM 2577 C SER B 149 16.677 37.238 49.198 1.00 41.91 B C ATOM 2578 O SER B 149 16.827 38.413 48.855 1.00 41.42 B O ATOM 2579 N ALA B 150 15.892 36.392 48.539 1.00 40.50 B N ATOM 2580 CA ALA B 150 15.229 36.802 47.308 1.00 40.10 B C ATOM 2581 CB ALA B 150 14.543 35.603 46.663 1.00 38.16 B C ATOM 2582 C ALA B 150 14.208 37.913 47.577 1.00 40.91 B C ATOM 2583 O ALA B 150 13.878 38.705 46.693 1.00 42.62 B O ATOM 2584 N VAL B 151 13.730 37.987 48.814 1.00 40.84 B N ATOM 2585 CA VAL B 151 12.567 38.794 49.133 1.00 37.46 B C ATOM 2586 CB VAL B 151 11.454 37.871 49.680 1.00 36.12 B C ATOM 2587 CG1 VAL B 151 11.031 36.897 48.607 1.00 33.40 B C ATOM 2588 CG2 VAL B 151 11.967 37.085 50.873 1.00 34.67 B C ATOM 2589 C VAL B 151 12.870 39.950 50.115 1.00 38.29 B C ATOM 2590 O VAL B 151 11.972 40.728 50.466 1.00 37.85 B O ATOM 2591 N THR B 152 14.130 40.062 50.545 1.00 39.26 B N ATOM 2592 CA THR B 152 14.560 41.107 51.499 1.00 41.68 B C ATOM 2593 CB THR B 152 14.935 40.509 52.908 1.00 43.62 B C ATOM 2594 OG1 THR B 152 16.052 39.614 52.784 1.00 45.98 B O ATOM 2595 CG2 THR B 152 13.760 39.741 53.510 1.00 44.83 B C ATOM 2596 C THR B 152 15.777 41.879 50.995 1.00 40.45 B C ATOM 2597 O THR B 152 16.537 41.373 50.178 1.00 42.39 B O ATOM 2598 N PRO B 153 15.976 43.115 51.478 1.00 39.85 B N ATOM 2599 CD PRO B 153 15.048 43.869 52.338 1.00 39.76 B C ATOM 2600 CA PRO B 153 17.180 43.895 51.167 1.00 40.14 B C ATOM 2601 CB PRO B 153 16.796 45.315 51.588 1.00 39.40 B C ATOM 2602 CG PRO B 153 15.814 45.113 52.696 1.00 39.26 B C ATOM 2603 C PRO B 153 18.436 43.385 51.914 1.00 40.82 B C ATOM 2604 O PRO B 153 19.340 44.161 52.241 1.00 41.47 B O ATOM 2605 N LEU B 154 18.474 42.085 52.198 1.00 39.77 B N ATOM 2606 CA LEU B 154 19.538 41.496 53.006 1.00 39.27 B C ATOM 2607 CB LEU B 154 18.925 40.962 54.305 1.00 40.72 B C ATOM 2608 CG LEU B 154 18.391 42.040 55.261 1.00 41.77 B C ATOM 2609 CD1 LEU B 154 17.327 41.461 56.196 1.00 40.29 B C ATOM 2610 CD2 LEU B 154 19.552 42.631 56.062 1.00 42.82 B C ATOM 2611 C LEU B 154 20.317 40.385 52.267 1.00 39.28 B C ATOM 2612 O LEU B 154 19.750 39.649 51.465 1.00 39.83 B O ATOM 2613 N THR B 155 21.621 40.285 52.521 1.00 39.08 B N ATOM 2614 CA THR B 155 22.404 39.155 52.039 1.00 39.68 B C ATOM 2615 CB THR B 155 23.542 39.567 51.028 1.00 39.54 B C ATOM 2616 OG1 THR B 155 24.547 40.331 51.705 1.00 40.29 B O ATOM 2617 CG2 THR B 155 22.979 40.375 49.866 1.00 38.14 B C ATOM 2618 C THR B 155 23.046 38.450 53.237 1.00 40.60 B C ATOM 2619 O THR B 155 23.384 39.084 54.234 1.00 42.13 B O ATOM 2620 N PHE B 156 23.210 37.136 53.128 1.00 41.65 B N ATOM 2621 CA PHE B 156 23.739 36.328 54.208 1.00 42.33 B C ATOM 2622 CB PHE B 156 22.738 35.217 54.556 1.00 40.59 B C ATOM 2623 CG PHE B 156 21.398 35.740 54.968 1.00 39.96 B C ATOM 2624 CD1 PHE B 156 20.447 36.075 54.009 1.00 39.88 B C ATOM 2625 CD2 PHE B 156 21.118 35.991 56.297 1.00 39.43 B C ATOM 2626 CE1 PHE B 156 19.236 36.665 54.362 1.00 40.60 B C ATOM 2627 CE2 PHE B 156 19.912 36.580 56.659 1.00 40.90 B C ATOM 2628 CZ PHE B 156 18.967 36.920 55.684 1.00 40.26 B C ATOM 2629 C PHE B 156 25.079 35.749 53.790 1.00 42.95 B C ATOM 2630 O PHE B 156 25.253 35.335 52.641 1.00 44.03 B O ATOM 2631 N THR B 157 26.028 35.750 54.723 1.00 44.29 B N ATOM 2632 CA THR B 157 27.359 35.204 54.488 1.00 44.28 B C ATOM 2633 CB THR B 157 28.413 36.302 54.369 1.00 45.00 B C ATOM 2634 OG1 THR B 157 28.275 36.971 53.108 1.00 45.30 B O ATOM 2635 CG2 THR B 157 29.819 35.699 54.484 1.00 46.04 B C ATOM 2636 C THR B 157 27.761 34.329 55.650 1.00 46.00 B C ATOM 2637 O THR B 157 27.568 34.698 56.814 1.00 48.07 B O ATOM 2638 N ARG B 158 28.340 33.177 55.331 1.00 45.97 B N ATOM 2639 CA ARG B 158 28.732 32.198 56.345 1.00 45.91 B C ATOM 2640 CB ARG B 158 28.703 30.790 55.748 1.00 45.97 B C ATOM 2641 CG ARG B 158 29.564 29.786 56.478 1.00 47.19 B C ATOM 2642 CD ARG B 158 28.717 28.727 57.140 1.00 48.18 B C ATOM 2643 NE ARG B 158 29.417 27.447 57.202 1.00 48.81 B N ATOM 2644 CZ ARG B 158 29.872 26.799 56.137 1.00 48.20 B C ATOM 2645 NH1 ARG B 158 29.703 27.318 54.926 1.00 46.73 B N ATOM 2646 NH2 ARG B 158 30.483 25.630 56.285 1.00 49.45 B N ATOM 2647 C ARG B 158 30.126 32.502 56.858 1.00 44.47 B C ATOM 2648 O ARG B 158 31.044 32.724 56.070 1.00 43.24 B O ATOM 2649 N VAL B 159 30.273 32.504 58.181 1.00 44.42 B N ATOM 2650 CA VAL B 159 31.552 32.805 58.823 1.00 43.12 B C ATOM 2651 CB VAL B 159 31.486 34.138 59.549 1.00 41.66 B C ATOM 2652 CG1 VAL B 159 31.244 35.274 58.553 1.00 39.64 B C ATOM 2653 CG2 VAL B 159 30.378 34.081 60.563 1.00 42.97 B C ATOM 2654 C VAL B 159 31.936 31.740 59.837 1.00 44.11 B C ATOM 2655 O VAL B 159 31.071 31.034 60.362 1.00 44.87 B O ATOM 2656 N TYR B 160 33.235 31.640 60.129 1.00 46.71 B N ATOM 2657 CA TYR B 160 33.757 30.559 60.981 1.00 46.55 B C ATOM 2658 CB TYR B 160 34.877 29.819 60.227 1.00 44.82 B C ATOM 2659 CG TYR B 160 34.410 29.269 58.894 1.00 45.07 B C ATOM 2660 CD1 TYR B 160 34.407 30.059 57.753 1.00 44.90 B C ATOM 2661 CE1 TYR B 160 33.886 29.584 56.549 1.00 45.04 B C ATOM 2662 CD2 TYR B 160 33.890 27.988 58.795 1.00 45.45 B C ATOM 2663 CE2 TYR B 160 33.367 27.505 57.601 1.00 44.31 B C ATOM 2664 CZ TYR B 160 33.364 28.309 56.485 1.00 44.88 B C ATOM 2665 OH TYR B 160 32.807 27.847 55.314 1.00 43.80 B O ATOM 2666 C TYR B 160 34.234 30.941 62.399 1.00 46.43 B C ATOM 2667 O TYR B 160 34.797 30.111 63.090 1.00 48.62 B O ATOM 2668 N SER B 161 34.004 32.171 62.845 1.00 48.41 B N ATOM 2669 CA SER B 161 34.298 32.519 64.234 1.00 48.84 B C ATOM 2670 CB SER B 161 35.204 33.755 64.314 1.00 46.65 B C ATOM 2671 OG SER B 161 34.447 34.953 64.250 1.00 40.38 B O ATOM 2672 C SER B 161 32.971 32.820 64.924 1.00 52.40 B C ATOM 2673 O SER B 161 31.902 32.553 64.369 1.00 53.60 B O ATOM 2674 N ARG B 162 33.042 33.401 66.120 1.00 53.85 B N ATOM 2675 CA ARG B 162 31.844 33.737 66.882 1.00 54.08 B C ATOM 2676 CB ARG B 162 32.078 33.516 68.385 1.00 56.45 B C ATOM 2677 CG ARG B 162 32.989 34.540 69.074 1.00 58.02 B C ATOM 2678 CD ARG B 162 33.214 34.200 70.560 1.00 59.85 B C ATOM 2679 NE ARG B 162 34.239 33.173 70.762 1.00 64.12 B N ATOM 2680 CZ ARG B 162 33.990 31.878 70.969 1.00 65.95 B C ATOM 2681 NH1 ARG B 162 32.739 31.439 71.004 1.00 68.19 B N ATOM 2682 NH2 ARG B 162 34.994 31.020 71.150 1.00 65.71 B N ATOM 2683 C ARG B 162 31.420 35.175 66.615 1.00 53.39 B C ATOM 2684 O ARG B 162 30.364 35.607 67.074 1.00 53.56 B O ATOM 2685 N ASP B 163 32.255 35.914 65.880 1.00 53.54 B N ATOM 2686 CA ASP B 163 31.819 37.154 65.216 1.00 53.03 B C ATOM 2687 CB ASP B 163 33.017 37.881 64.564 1.00 55.49 B C ATOM 2688 CG ASP B 163 32.591 39.013 63.591 1.00 59.41 B C ATOM 2689 OD1 ASP B 163 31.453 39.532 63.704 1.00 59.92 B O ATOM 2690 OD2 ASP B 163 33.407 39.386 62.708 1.00 60.18 B O ATOM 2691 C ASP B 163 30.815 36.738 64.146 1.00 50.79 B C ATOM 2692 O ASP B 163 31.195 36.351 63.038 1.00 49.93 B O ATOM 2693 N ALA B 164 29.535 36.799 64.495 1.00 48.01 B N ATOM 2694 CA ALA B 164 28.495 36.312 63.609 1.00 46.93 B C ATOM 2695 CB ALA B 164 28.576 34.790 63.494 1.00 46.17 B C ATOM 2696 C ALA B 164 27.118 36.726 64.097 1.00 46.34 B C ATOM 2697 O ALA B 164 26.702 36.385 65.205 1.00 46.04 B O ATOM 2698 N ASP B 165 26.414 37.473 63.258 1.00 46.17 B N ATOM 2699 CA ASP B 165 25.096 37.965 63.609 1.00 46.11 B C ATOM 2700 CB ASP B 165 24.430 38.609 62.399 1.00 46.15 B C ATOM 2701 CG ASP B 165 25.151 39.853 61.943 1.00 48.04 B C ATOM 2702 OD1 ASP B 165 25.656 40.595 62.827 1.00 48.57 B O ATOM 2703 OD2 ASP B 165 25.209 40.086 60.711 1.00 46.91 B O ATOM 2704 C ASP B 165 24.246 36.818 64.101 1.00 45.99 B C ATOM 2705 O ASP B 165 23.613 36.937 65.132 1.00 48.67 B O ATOM 2706 N ILE B 166 24.233 35.711 63.363 1.00 44.71 B N ATOM 2707 CA ILE B 166 23.473 34.538 63.769 1.00 42.89 B C ATOM 2708 CB ILE B 166 22.426 34.150 62.681 1.00 44.84 B C ATOM 2709 CG2 ILE B 166 21.816 32.761 63.004 1.00 45.20 B C ATOM 2710 CG1 ILE B 166 21.356 35.258 62.580 1.00 45.57 B C ATOM 2711 CD1 ILE B 166 20.201 35.018 61.572 1.00 43.21 B C ATOM 2712 C ILE B 166 24.357 33.321 64.090 1.00 41.58 B C ATOM 2713 O ILE B 166 25.116 32.838 63.246 1.00 40.06 B O ATOM 2714 N VAL B 167 24.254 32.833 65.328 1.00 41.03 B N ATOM 2715 CA VAL B 167 24.960 31.620 65.738 1.00 38.97 B C ATOM 2716 CB VAL B 167 25.578 31.786 67.127 1.00 36.64 B C ATOM 2717 CG1 VAL B 167 26.258 30.504 67.544 1.00 35.82 B C ATOM 2718 CG2 VAL B 167 26.572 32.919 67.104 1.00 34.72 B C ATOM 2719 C VAL B 167 24.016 30.424 65.741 1.00 41.07 B C ATOM 2720 O VAL B 167 22.954 30.463 66.367 1.00 40.50 B O ATOM 2721 N ILE B 168 24.404 29.368 65.028 1.00 40.78 B N ATOM 2722 CA ILE B 168 23.550 28.193 64.882 1.00 41.64 B C ATOM 2723 CB ILE B 168 23.434 27.802 63.402 1.00 42.63 B C ATOM 2724 CG2 ILE B 168 22.669 26.500 63.266 1.00 41.44 B C ATOM 2725 CG1 ILE B 168 22.754 28.943 62.631 1.00 42.77 B C ATOM 2726 CD1 ILE B 168 22.265 28.557 61.246 1.00 42.40 B C ATOM 2727 C ILE B 168 24.038 26.988 65.693 1.00 43.33 B C ATOM 2728 O ILE B 168 25.211 26.647 65.639 1.00 45.09 B O ATOM 2729 N GLN B 169 23.147 26.344 66.444 1.00 43.40 B N ATOM 2730 CA GLN B 169 23.568 25.262 67.335 1.00 44.15 B C ATOM 2731 CB GLN B 169 23.865 25.840 68.716 1.00 45.30 B C ATOM 2732 CG GLN B 169 24.242 24.804 69.757 1.00 47.04 B C ATOM 2733 CD GLN B 169 23.776 25.194 71.163 1.00 48.16 B C ATOM 2734 OE1 GLN B 169 23.775 26.375 71.519 1.00 48.37 B O ATOM 2735 NE2 GLN B 169 23.376 24.201 71.962 1.00 47.14 B N ATOM 2736 C GLN B 169 22.579 24.091 67.478 1.00 44.06 B C ATOM 2737 O GLN B 169 21.396 24.285 67.758 1.00 44.73 B O ATOM 2738 N PHE B 170 23.070 22.870 67.303 1.00 43.03 B N ATOM 2739 CA PHE B 170 22.287 21.705 67.695 1.00 43.87 B C ATOM 2740 CB PHE B 170 22.693 20.476 66.874 1.00 42.71 B C ATOM 2741 CG PHE B 170 22.324 20.549 65.416 1.00 42.43 B C ATOM 2742 CD1 PHE B 170 23.231 21.053 64.483 1.00 41.71 B C ATOM 2743 CD2 PHE B 170 21.098 20.041 64.966 1.00 42.38 B C ATOM 2744 CE1 PHE B 170 22.934 21.045 63.129 1.00 40.51 B C ATOM 2745 CE2 PHE B 170 20.781 20.025 63.613 1.00 40.13 B C ATOM 2746 CZ PHE B 170 21.703 20.526 62.689 1.00 41.47 B C ATOM 2747 C PHE B 170 22.521 21.424 69.191 1.00 44.46 B C ATOM 2748 O PHE B 170 23.639 21.549 69.683 1.00 42.66 B O ATOM 2749 N GLY B 171 21.476 21.045 69.913 1.00 44.65 B N ATOM 2750 CA GLY B 171 21.653 20.759 71.323 1.00 47.14 B C ATOM 2751 C GLY B 171 20.581 19.819 71.838 1.00 49.17 B C ATOM 2752 O GLY B 171 19.590 19.563 71.144 1.00 50.35 B O ATOM 2753 N VAL B 172 20.767 19.297 73.049 1.00 48.87 B N ATOM 2754 CA VAL B 172 19.712 18.527 73.723 1.00 49.12 B C ATOM 2755 CB VAL B 172 20.075 17.016 73.816 1.00 46.61 B C ATOM 2756 CG1 VAL B 172 20.014 16.374 72.446 1.00 43.45 B C ATOM 2757 CG2 VAL B 172 21.447 16.846 74.433 1.00 43.17 B C ATOM 2758 C VAL B 172 19.386 19.032 75.142 1.00 50.61 B C ATOM 2759 O VAL B 172 20.224 19.655 75.804 1.00 51.06 B O ATOM 2760 N ALA B 173 18.161 18.771 75.603 1.00 51.57 B N ATOM 2761 CA ALA B 173 17.776 19.118 76.975 1.00 51.58 B C ATOM 2762 CB ALA B 173 18.551 18.256 77.959 1.00 49.61 B C ATOM 2763 C ALA B 173 18.056 20.599 77.236 1.00 52.82 B C ATOM 2764 O ALA B 173 17.649 21.465 76.456 1.00 53.31 B O ATOM 2765 N GLU B 174 18.759 20.887 78.331 1.00 54.71 B N ATOM 2766 CA GLU B 174 19.239 22.242 78.621 1.00 53.26 B C ATOM 2767 CB GLU B 174 19.364 22.464 80.128 1.00 55.77 B C ATOM 2768 CG GLU B 174 19.588 23.911 80.497 1.00 59.80 B C ATOM 2769 CD GLU B 174 18.461 24.802 79.988 1.00 62.99 B C ATOM 2770 OE1 GLU B 174 17.729 25.374 80.837 1.00 63.97 B O ATOM 2771 OE2 GLU B 174 18.304 24.924 78.740 1.00 64.84 B O ATOM 2772 C GLU B 174 20.601 22.443 77.984 1.00 51.98 B C ATOM 2773 O GLU B 174 21.539 21.678 78.229 1.00 51.97 B O ATOM 2774 N HIS B 175 20.705 23.483 77.170 1.00 50.90 B N ATOM 2775 CA HIS B 175 21.874 23.670 76.329 1.00 49.30 B C ATOM 2776 CB HIS B 175 21.481 23.505 74.857 1.00 48.17 B C ATOM 2777 CG HIS B 175 20.173 24.143 74.493 1.00 47.43 B C ATOM 2778 CD2 HIS B 175 19.772 25.435 74.508 1.00 46.86 B C ATOM 2779 ND1 HIS B 175 19.101 23.416 74.017 1.00 47.66 B N ATOM 2780 CE1 HIS B 175 18.097 24.234 73.757 1.00 45.86 B C ATOM 2781 NE2 HIS B 175 18.478 25.464 74.046 1.00 45.27 B N ATOM 2782 C HIS B 175 22.530 25.023 76.575 1.00 48.32 B C ATOM 2783 O HIS B 175 23.354 25.492 75.783 1.00 48.12 B O ATOM 2784 N GLY B 176 22.152 25.649 77.685 1.00 48.13 B N ATOM 2785 CA GLY B 176 22.850 26.839 78.134 1.00 47.35 B C ATOM 2786 C GLY B 176 22.174 28.125 77.725 1.00 46.62 B C ATOM 2787 O GLY B 176 22.850 29.094 77.393 1.00 46.34 B O ATOM 2788 N ASP B 177 20.841 28.129 77.740 1.00 47.01 B N ATOM 2789 CA ASP B 177 20.078 29.362 77.589 1.00 47.08 B C ATOM 2790 CB ASP B 177 19.735 29.622 76.118 1.00 46.99 B C ATOM 2791 CG ASP B 177 18.773 28.599 75.530 1.00 47.26 B C ATOM 2792 OD1 ASP B 177 18.264 27.725 76.281 1.00 46.52 B O ATOM 2793 OD2 ASP B 177 18.532 28.689 74.295 1.00 45.00 B O ATOM 2794 C ASP B 177 18.814 29.351 78.428 1.00 47.30 B C ATOM 2795 O ASP B 177 17.958 30.237 78.315 1.00 46.18 B O ATOM 2796 N GLY B 178 18.709 28.334 79.273 1.00 47.82 B N ATOM 2797 CA GLY B 178 17.617 28.293 80.219 1.00 49.94 B C ATOM 2798 C GLY B 178 16.286 28.034 79.543 1.00 50.90 B C ATOM 2799 O GLY B 178 15.233 28.089 80.179 1.00 53.83 B O ATOM 2800 N TYR B 179 16.319 27.755 78.246 1.00 50.73 B N ATOM 2801 CA TYR B 179 15.105 27.377 77.531 1.00 48.38 B C ATOM 2802 CB TYR B 179 14.805 28.371 76.421 1.00 47.06 B C ATOM 2803 CG TYR B 179 14.385 29.736 76.919 1.00 46.64 B C ATOM 2804 CD1 TYR B 179 15.332 30.699 77.249 1.00 45.72 B C ATOM 2805 CE1 TYR B 179 14.955 31.971 77.632 1.00 45.55 B C ATOM 2806 CD2 TYR B 179 13.043 30.083 76.996 1.00 47.09 B C ATOM 2807 CE2 TYR B 179 12.657 31.353 77.375 1.00 46.89 B C ATOM 2808 CZ TYR B 179 13.616 32.294 77.688 1.00 46.35 B C ATOM 2809 OH TYR B 179 13.216 33.569 78.027 1.00 47.43 B O ATOM 2810 C TYR B 179 15.293 25.993 76.952 1.00 47.71 B C ATOM 2811 O TYR B 179 15.416 25.816 75.741 1.00 46.97 B O ATOM 2812 N PRO B 180 15.308 24.987 77.831 1.00 46.25 B N ATOM 2813 CD PRO B 180 14.864 25.149 79.224 1.00 44.90 B C ATOM 2814 CA PRO B 180 15.677 23.606 77.531 1.00 45.55 B C ATOM 2815 CB PRO B 180 15.724 22.955 78.897 1.00 45.49 B C ATOM 2816 CG PRO B 180 14.725 23.743 79.694 1.00 45.12 B C ATOM 2817 C PRO B 180 14.697 22.902 76.604 1.00 45.86 B C ATOM 2818 O PRO B 180 13.485 23.098 76.697 1.00 45.57 B O ATOM 2819 N PHE B 181 15.245 22.074 75.719 1.00 47.00 B N ATOM 2820 CA PHE B 181 14.468 21.166 74.874 1.00 48.31 B C ATOM 2821 CB PHE B 181 15.341 20.615 73.750 1.00 48.17 B C ATOM 2822 CG PHE B 181 15.771 21.647 72.757 1.00 46.35 B C ATOM 2823 CD1 PHE B 181 14.948 22.722 72.466 1.00 46.24 B C ATOM 2824 CD2 PHE B 181 16.989 21.530 72.103 1.00 45.59 B C ATOM 2825 CE1 PHE B 181 15.328 23.661 71.542 1.00 46.10 B C ATOM 2826 CE2 PHE B 181 17.372 22.463 71.181 1.00 45.25 B C ATOM 2827 CZ PHE B 181 16.537 23.536 70.896 1.00 45.48 B C ATOM 2828 C PHE B 181 13.872 19.985 75.633 1.00 49.27 B C ATOM 2829 O PHE B 181 14.165 19.765 76.810 1.00 50.37 B O ATOM 2830 N ASP B 182 13.050 19.209 74.931 1.00 50.07 B N ATOM 2831 CA ASP B 182 12.195 18.204 75.559 1.00 50.05 B C ATOM 2832 CB ASP B 182 10.727 18.648 75.470 1.00 50.98 B C ATOM 2833 CG ASP B 182 10.241 18.813 74.021 1.00 51.83 B C ATOM 2834 OD1 ASP B 182 10.998 19.352 73.189 1.00 51.17 B O ATOM 2835 OD2 ASP B 182 9.095 18.401 73.712 1.00 53.43 B O ATOM 2836 C ASP B 182 12.344 16.823 74.924 1.00 50.10 B C ATOM 2837 O ASP B 182 11.355 16.154 74.641 1.00 51.84 B O ATOM 2838 N GLY B 183 13.573 16.392 74.689 1.00 50.20 B N ATOM 2839 CA GLY B 183 13.758 15.078 74.108 1.00 50.19 B C ATOM 2840 C GLY B 183 13.178 14.962 72.715 1.00 49.89 B C ATOM 2841 O GLY B 183 13.595 15.669 71.802 1.00 50.71 B O ATOM 2842 N LYS B 184 12.213 14.072 72.539 1.00 50.71 B N ATOM 2843 CA LYS B 184 11.888 13.601 71.198 1.00 52.14 B C ATOM 2844 CB LYS B 184 12.177 12.100 71.113 1.00 53.44 B C ATOM 2845 CG LYS B 184 11.745 11.449 69.825 1.00 54.99 B C ATOM 2846 CD LYS B 184 11.534 9.963 70.043 1.00 57.13 B C ATOM 2847 CE LYS B 184 10.660 9.365 68.948 1.00 59.13 B C ATOM 2848 NZ LYS B 184 9.301 9.995 68.879 1.00 58.76 B N ATOM 2849 C LYS B 184 10.444 13.888 70.802 1.00 52.58 B C ATOM 2850 O LYS B 184 9.513 13.508 71.515 1.00 52.82 B O ATOM 2851 N ASP B 185 10.274 14.553 69.658 1.00 52.06 B N ATOM 2852 CA ASP B 185 8.982 15.084 69.236 1.00 51.37 B C ATOM 2853 CB ASP B 185 7.925 13.981 69.214 1.00 53.88 B C ATOM 2854 CG ASP B 185 8.316 12.818 68.309 1.00 56.84 B C ATOM 2855 OD1 ASP B 185 9.288 12.977 67.523 1.00 58.84 B O ATOM 2856 OD2 ASP B 185 7.649 11.756 68.378 1.00 56.58 B O ATOM 2857 C ASP B 185 8.560 16.181 70.195 1.00 50.45 B C ATOM 2858 O ASP B 185 9.216 16.418 71.203 1.00 51.04 B O ATOM 2859 N GLY B 186 7.452 16.846 69.903 1.00 49.96 B N ATOM 2860 CA GLY B 186 7.085 18.002 70.702 1.00 47.71 B C ATOM 2861 C GLY B 186 7.642 19.243 70.041 1.00 47.77 B C ATOM 2862 O GLY B 186 7.371 19.508 68.868 1.00 47.87 B O ATOM 2863 N LEU B 187 8.424 20.023 70.770 1.00 47.62 B N ATOM 2864 CA LEU B 187 9.015 21.181 70.132 1.00 48.61 B C ATOM 2865 CB LEU B 187 9.212 22.329 71.139 1.00 48.72 B C ATOM 2866 CG LEU B 187 9.704 22.063 72.556 1.00 47.44 B C ATOM 2867 CD1 LEU B 187 10.320 23.325 73.114 1.00 46.61 B C ATOM 2868 CD2 LEU B 187 8.549 21.590 73.422 1.00 47.68 B C ATOM 2869 C LEU B 187 10.343 20.788 69.473 1.00 48.13 B C ATOM 2870 O LEU B 187 11.238 20.268 70.126 1.00 48.94 B O ATOM 2871 N LEU B 188 10.446 21.037 68.171 1.00 45.28 B N ATOM 2872 CA LEU B 188 11.602 20.655 67.386 1.00 41.64 B C ATOM 2873 CB LEU B 188 11.213 20.591 65.914 1.00 42.63 B C ATOM 2874 CG LEU B 188 10.040 19.662 65.583 1.00 42.15 B C ATOM 2875 CD1 LEU B 188 9.613 19.869 64.137 1.00 41.06 B C ATOM 2876 CD2 LEU B 188 10.453 18.223 65.820 1.00 41.02 B C ATOM 2877 C LEU B 188 12.775 21.614 67.562 1.00 40.89 B C ATOM 2878 O LEU B 188 13.928 21.182 67.610 1.00 41.38 B O ATOM 2879 N ALA B 189 12.480 22.911 67.653 1.00 38.67 B N ATOM 2880 CA ALA B 189 13.506 23.949 67.762 1.00 35.47 B C ATOM 2881 CB ALA B 189 14.267 24.049 66.475 1.00 35.61 B C ATOM 2882 C ALA B 189 12.925 25.307 68.105 1.00 35.91 B C ATOM 2883 O ALA B 189 11.715 25.504 68.113 1.00 35.15 B O ATOM 2884 N HIS B 190 13.796 26.257 68.394 1.00 37.57 B N ATOM 2885 CA HIS B 190 13.361 27.640 68.431 1.00 39.50 B C ATOM 2886 CB HIS B 190 12.932 28.027 69.847 1.00 41.66 B C ATOM 2887 CG HIS B 190 13.970 27.777 70.897 1.00 42.26 B C ATOM 2888 CD2 HIS B 190 15.203 28.309 71.084 1.00 43.73 B C ATOM 2889 ND1 HIS B 190 13.762 26.918 71.952 1.00 42.74 B N ATOM 2890 CE1 HIS B 190 14.818 26.930 72.745 1.00 42.32 B C ATOM 2891 NE2 HIS B 190 15.707 27.768 72.242 1.00 42.46 B N ATOM 2892 C HIS B 190 14.431 28.587 67.920 1.00 40.35 B C ATOM 2893 O HIS B 190 15.446 28.153 67.374 1.00 41.11 B O ATOM 2894 N ALA B 191 14.194 29.883 68.085 1.00 40.39 B N ATOM 2895 CA ALA B 191 15.114 30.906 67.584 1.00 42.00 B C ATOM 2896 CB ALA B 191 14.919 31.093 66.073 1.00 39.51 B C ATOM 2897 C ALA B 191 14.896 32.236 68.308 1.00 42.12 B C ATOM 2898 O ALA B 191 13.780 32.559 68.685 1.00 42.59 B O ATOM 2899 N PHE B 192 15.961 33.005 68.494 1.00 42.45 B N ATOM 2900 CA PHE B 192 15.841 34.290 69.168 1.00 43.53 B C ATOM 2901 CB PHE B 192 17.054 34.519 70.047 1.00 44.53 B C ATOM 2902 CG PHE B 192 17.060 33.651 71.249 1.00 44.83 B C ATOM 2903 CD1 PHE B 192 16.503 34.091 72.433 1.00 44.75 B C ATOM 2904 CD2 PHE B 192 17.578 32.374 71.188 1.00 46.15 B C ATOM 2905 CE1 PHE B 192 16.457 33.277 73.537 1.00 43.76 B C ATOM 2906 CE2 PHE B 192 17.537 31.548 72.291 1.00 46.52 B C ATOM 2907 CZ PHE B 192 16.973 32.004 73.469 1.00 45.40 B C ATOM 2908 C PHE B 192 15.658 35.462 68.212 1.00 44.86 B C ATOM 2909 O PHE B 192 15.971 35.359 67.016 1.00 46.32 B O ATOM 2910 N PRO B 193 15.128 36.590 68.716 1.00 43.32 B N ATOM 2911 CD PRO B 193 14.565 36.775 70.062 1.00 41.27 B C ATOM 2912 CA PRO B 193 14.904 37.751 67.841 1.00 43.10 B C ATOM 2913 CB PRO B 193 13.970 38.654 68.662 1.00 42.03 B C ATOM 2914 CG PRO B 193 14.175 38.223 70.076 1.00 42.25 B C ATOM 2915 C PRO B 193 16.218 38.450 67.422 1.00 42.87 B C ATOM 2916 O PRO B 193 17.269 38.244 68.029 1.00 43.53 B O ATOM 2917 N PRO B 194 16.174 39.275 66.359 1.00 43.68 B N ATOM 2918 CD PRO B 194 15.074 39.523 65.401 1.00 42.33 B C ATOM 2919 CA PRO B 194 17.422 39.943 65.956 1.00 42.55 B C ATOM 2920 CB PRO B 194 17.030 40.707 64.687 1.00 42.22 B C ATOM 2921 CG PRO B 194 15.808 39.991 64.166 1.00 41.34 B C ATOM 2922 C PRO B 194 17.915 40.878 67.054 1.00 43.26 B C ATOM 2923 O PRO B 194 17.140 41.677 67.586 1.00 43.12 B O ATOM 2924 N GLY B 195 19.196 40.797 67.397 1.00 43.58 B N ATOM 2925 CA GLY B 195 19.711 41.704 68.415 1.00 45.49 B C ATOM 2926 C GLY B 195 21.146 41.435 68.819 1.00 45.92 B C ATOM 2927 O GLY B 195 21.861 40.753 68.099 1.00 45.73 B O ATOM 2928 N PRO B 196 21.600 41.969 69.961 1.00 45.58 B N ATOM 2929 CD PRO B 196 20.900 42.984 70.772 1.00 45.79 B C ATOM 2930 CA PRO B 196 22.896 41.592 70.542 1.00 46.21 B C ATOM 2931 CB PRO B 196 23.109 42.623 71.649 1.00 46.39 B C ATOM 2932 CG PRO B 196 21.708 43.024 72.048 1.00 46.25 B C ATOM 2933 C PRO B 196 22.868 40.176 71.099 1.00 46.39 B C ATOM 2934 O PRO B 196 21.806 39.662 71.438 1.00 47.42 B O ATOM 2935 N GLY B 197 24.035 39.541 71.181 1.00 47.78 B N ATOM 2936 CA GLY B 197 24.197 38.358 72.030 1.00 47.25 B C ATOM 2937 C GLY B 197 23.617 37.024 71.570 1.00 46.37 B C ATOM 2938 O GLY B 197 23.979 36.490 70.532 1.00 46.15 B O ATOM 2939 N ILE B 198 22.732 36.467 72.386 1.00 47.41 B N ATOM 2940 CA ILE B 198 21.989 35.272 72.021 1.00 47.27 B C ATOM 2941 CB ILE B 198 21.327 34.638 73.229 1.00 48.66 B C ATOM 2942 CG2 ILE B 198 20.259 35.587 73.787 1.00 47.22 B C ATOM 2943 CG1 ILE B 198 20.660 33.327 72.818 1.00 50.98 B C ATOM 2944 CD1 ILE B 198 21.583 32.439 71.983 1.00 52.70 B C ATOM 2945 C ILE B 198 20.855 35.671 71.088 1.00 47.61 B C ATOM 2946 O ILE B 198 20.154 34.819 70.538 1.00 48.77 B O ATOM 2947 N GLN B 199 20.638 36.972 70.946 1.00 46.21 B N ATOM 2948 CA GLN B 199 19.559 37.416 70.098 1.00 44.85 B C ATOM 2949 CB GLN B 199 19.221 38.882 70.387 1.00 44.49 B C ATOM 2950 CG GLN B 199 18.401 39.075 71.676 1.00 44.73 B C ATOM 2951 CD GLN B 199 18.210 40.553 72.065 1.00 47.27 B C ATOM 2952 OE1 GLN B 199 17.855 41.390 71.223 1.00 47.82 B O ATOM 2953 NE2 GLN B 199 18.452 40.874 73.345 1.00 46.28 B N ATOM 2954 C GLN B 199 20.022 37.216 68.664 1.00 43.90 B C ATOM 2955 O GLN B 199 20.925 37.893 68.208 1.00 44.67 B O ATOM 2956 N GLY B 200 19.429 36.248 67.973 1.00 42.93 B N ATOM 2957 CA GLY B 200 19.710 36.075 66.561 1.00 43.21 B C ATOM 2958 C GLY B 200 20.076 34.639 66.248 1.00 45.16 B C ATOM 2959 O GLY B 200 20.135 34.211 65.081 1.00 44.33 B O ATOM 2960 N ASP B 201 20.318 33.893 67.319 1.00 44.98 B N ATOM 2961 CA ASP B 201 20.574 32.462 67.249 1.00 45.36 B C ATOM 2962 CB ASP B 201 21.110 31.974 68.601 1.00 46.30 B C ATOM 2963 CG ASP B 201 22.549 32.343 68.829 1.00 47.35 B C ATOM 2964 OD1 ASP B 201 22.987 33.427 68.369 1.00 49.22 B O ATOM 2965 OD2 ASP B 201 23.247 31.537 69.483 1.00 47.81 B O ATOM 2966 C ASP B 201 19.339 31.623 66.867 1.00 45.46 B C ATOM 2967 O ASP B 201 18.182 32.007 67.101 1.00 45.37 B O ATOM 2968 N ALA B 202 19.619 30.459 66.286 1.00 44.34 B N ATOM 2969 CA ALA B 202 18.613 29.449 65.994 1.00 41.65 B C ATOM 2970 CB ALA B 202 18.272 29.478 64.501 1.00 40.80 B C ATOM 2971 C ALA B 202 19.153 28.075 66.393 1.00 39.53 B C ATOM 2972 O ALA B 202 20.170 27.618 65.876 1.00 38.32 B O ATOM 2973 N HIS B 203 18.460 27.429 67.321 1.00 40.41 B N ATOM 2974 CA HIS B 203 18.867 26.133 67.860 1.00 40.01 B C ATOM 2975 CB HIS B 203 18.806 26.181 69.386 1.00 39.51 B C ATOM 2976 CG HIS B 203 19.661 27.258 69.979 1.00 40.38 B C ATOM 2977 CD2 HIS B 203 20.905 27.682 69.655 1.00 40.75 B C ATOM 2978 ND1 HIS B 203 19.260 28.030 71.048 1.00 41.15 B N ATOM 2979 CE1 HIS B 203 20.222 28.879 71.358 1.00 41.02 B C ATOM 2980 NE2 HIS B 203 21.232 28.689 70.529 1.00 40.36 B N ATOM 2981 C HIS B 203 17.971 25.019 67.352 1.00 39.63 B C ATOM 2982 O HIS B 203 16.814 25.252 67.005 1.00 40.31 B O ATOM 2983 N PHE B 204 18.501 23.804 67.317 1.00 39.56 B N ATOM 2984 CA PHE B 204 17.739 22.667 66.816 1.00 38.07 B C ATOM 2985 CB PHE B 204 18.260 22.272 65.432 1.00 38.92 B C ATOM 2986 CG PHE B 204 18.193 23.388 64.433 1.00 38.34 B C ATOM 2987 CD1 PHE B 204 19.191 24.339 64.372 1.00 36.69 B C ATOM 2988 CD2 PHE B 204 17.098 23.519 63.593 1.00 38.44 B C ATOM 2989 CE1 PHE B 204 19.090 25.394 63.500 1.00 37.05 B C ATOM 2990 CE2 PHE B 204 17.005 24.583 62.721 1.00 37.27 B C ATOM 2991 CZ PHE B 204 17.996 25.518 62.673 1.00 35.10 B C ATOM 2992 C PHE B 204 17.848 21.491 67.758 1.00 37.48 B C ATOM 2993 O PHE B 204 18.947 21.099 68.146 1.00 35.94 B O ATOM 2994 N ASP B 205 16.705 20.923 68.122 1.00 38.68 B N ATOM 2995 CA ASP B 205 16.696 19.754 68.994 1.00 41.03 B C ATOM 2996 CB ASP B 205 15.271 19.463 69.466 1.00 41.80 B C ATOM 2997 CG ASP B 205 15.238 18.467 70.599 1.00 43.94 B C ATOM 2998 OD1 ASP B 205 16.122 17.573 70.622 1.00 45.36 B O ATOM 2999 OD2 ASP B 205 14.343 18.577 71.462 1.00 42.56 B O ATOM 3000 C ASP B 205 17.293 18.500 68.327 1.00 42.68 B C ATOM 3001 O ASP B 205 16.708 17.927 67.405 1.00 41.40 B O ATOM 3002 N ASP B 206 18.459 18.076 68.807 1.00 44.32 B N ATOM 3003 CA ASP B 206 19.223 17.038 68.122 1.00 46.24 B C ATOM 3004 CB ASP B 206 20.738 17.279 68.282 1.00 48.63 B C ATOM 3005 CG ASP B 206 21.580 16.503 67.249 1.00 51.32 B C ATOM 3006 OD1 ASP B 206 20.999 15.689 66.498 1.00 54.26 B O ATOM 3007 OD2 ASP B 206 22.821 16.702 67.186 1.00 52.05 B O ATOM 3008 C ASP B 206 18.847 15.681 68.688 1.00 46.87 B C ATOM 3009 O ASP B 206 19.464 14.666 68.367 1.00 47.41 B O ATOM 3010 N ASP B 207 17.830 15.673 69.542 1.00 47.41 B N ATOM 3011 CA ASP B 207 17.226 14.428 69.984 1.00 48.07 B C ATOM 3012 CB ASP B 207 16.445 14.649 71.290 1.00 48.89 B C ATOM 3013 CG ASP B 207 17.312 14.441 72.543 1.00 51.54 B C ATOM 3014 OD1 ASP B 207 18.193 13.540 72.516 1.00 51.22 B O ATOM 3015 OD2 ASP B 207 17.101 15.171 73.552 1.00 51.89 B O ATOM 3016 C ASP B 207 16.307 13.941 68.866 1.00 48.06 B C ATOM 3017 O ASP B 207 15.897 12.776 68.826 1.00 48.72 B O ATOM 3018 N GLU B 208 16.014 14.844 67.940 1.00 47.98 B N ATOM 3019 CA GLU B 208 15.233 14.519 66.753 1.00 48.39 B C ATOM 3020 CB GLU B 208 14.458 15.767 66.311 1.00 49.39 B C ATOM 3021 CG GLU B 208 13.792 16.504 67.460 1.00 49.24 B C ATOM 3022 CD GLU B 208 12.541 15.811 67.926 1.00 50.52 B C ATOM 3023 OE1 GLU B 208 12.505 14.559 67.947 1.00 50.44 B O ATOM 3024 OE2 GLU B 208 11.577 16.522 68.264 1.00 52.60 B O ATOM 3025 C GLU B 208 16.106 14.011 65.593 1.00 47.48 B C ATOM 3026 O GLU B 208 17.298 14.311 65.522 1.00 48.26 B O ATOM 3027 N LEU B 209 15.494 13.244 64.691 1.00 47.58 B N ATOM 3028 CA LEU B 209 16.144 12.776 63.464 1.00 47.23 B C ATOM 3029 CB LEU B 209 15.552 11.449 63.026 1.00 46.79 B C ATOM 3030 CG LEU B 209 15.925 11.064 61.600 1.00 47.21 B C ATOM 3031 CD1 LEU B 209 17.374 10.535 61.572 1.00 46.54 B C ATOM 3032 CD2 LEU B 209 14.949 10.004 61.090 1.00 45.83 B C ATOM 3033 C LEU B 209 15.965 13.778 62.330 1.00 47.66 B C ATOM 3034 O LEU B 209 14.837 14.106 61.952 1.00 48.63 B O ATOM 3035 N TRP B 210 17.074 14.261 61.784 1.00 46.14 B N ATOM 3036 CA TRP B 210 17.006 15.306 60.781 1.00 44.12 B C ATOM 3037 CB TRP B 210 18.008 16.427 61.118 1.00 41.71 B C ATOM 3038 CG TRP B 210 17.540 17.268 62.318 1.00 40.65 B C ATOM 3039 CD2 TRP B 210 16.409 18.162 62.359 1.00 38.29 B C ATOM 3040 CE2 TRP B 210 16.272 18.611 63.690 1.00 38.00 B C ATOM 3041 CE3 TRP B 210 15.495 18.619 61.398 1.00 35.91 B C ATOM 3042 CD1 TRP B 210 18.035 17.232 63.602 1.00 39.20 B C ATOM 3043 NE1 TRP B 210 17.274 18.032 64.428 1.00 37.89 B N ATOM 3044 CZ2 TRP B 210 15.267 19.484 64.082 1.00 38.51 B C ATOM 3045 CZ3 TRP B 210 14.499 19.484 61.782 1.00 35.66 B C ATOM 3046 CH2 TRP B 210 14.387 19.909 63.112 1.00 38.82 B C ATOM 3047 C TRP B 210 17.271 14.683 59.428 1.00 45.10 B C ATOM 3048 O TRP B 210 17.912 13.641 59.337 1.00 45.75 B O ATOM 3049 N SER B 211 16.736 15.292 58.378 1.00 46.33 B N ATOM 3050 CA SER B 211 16.876 14.753 57.023 1.00 47.47 B C ATOM 3051 CB SER B 211 16.144 13.395 56.893 1.00 45.60 B C ATOM 3052 OG SER B 211 14.821 13.410 57.408 1.00 40.76 B O ATOM 3053 C SER B 211 16.334 15.751 56.007 1.00 48.99 B C ATOM 3054 O SER B 211 16.057 16.900 56.357 1.00 50.58 B O ATOM 3055 N LEU B 212 16.200 15.318 54.755 1.00 50.28 B N ATOM 3056 CA LEU B 212 15.498 16.095 53.731 1.00 50.77 B C ATOM 3057 CB LEU B 212 15.735 15.478 52.359 1.00 52.04 B C ATOM 3058 CG LEU B 212 17.216 15.348 51.978 1.00 52.93 B C ATOM 3059 CD1 LEU B 212 17.352 14.601 50.637 1.00 51.42 B C ATOM 3060 CD2 LEU B 212 17.837 16.749 51.914 1.00 51.71 B C ATOM 3061 C LEU B 212 13.995 16.183 53.994 1.00 52.40 B C ATOM 3062 O LEU B 212 13.399 17.230 53.780 1.00 52.79 B O ATOM 3063 N GLY B 213 13.379 15.092 54.448 1.00 54.59 B N ATOM 3064 CA GLY B 213 12.034 15.190 54.997 1.00 55.70 B C ATOM 3065 C GLY B 213 10.977 14.294 54.373 1.00 57.19 B C ATOM 3066 O GLY B 213 9.774 14.422 54.672 1.00 58.02 B O ATOM 3067 N LYS B 389 11.424 13.383 53.506 1.00 58.33 B N ATOM 3068 CA LYS B 389 10.526 12.481 52.752 1.00 58.43 B C ATOM 3069 CB LYS B 389 11.027 12.329 51.305 1.00 57.68 B C ATOM 3070 CG LYS B 389 11.006 13.614 50.488 1.00 58.29 B C ATOM 3071 CD LYS B 389 12.100 13.633 49.414 1.00 59.54 B C ATOM 3072 CE LYS B 389 13.481 13.295 50.009 1.00 62.11 B C ATOM 3073 NZ LYS B 389 14.656 13.669 49.143 1.00 63.74 B N ATOM 3074 C LYS B 389 10.393 11.088 53.384 1.00 58.26 B C ATOM 3075 O LYS B 389 9.598 10.278 52.920 1.00 57.88 B O ATOM 3076 N GLY B 390 11.192 10.819 54.419 1.00 59.12 B N ATOM 3077 CA GLY B 390 11.110 9.553 55.125 1.00 58.22 B C ATOM 3078 C GLY B 390 10.361 9.707 56.439 1.00 58.66 B C ATOM 3079 O GLY B 390 9.157 9.954 56.453 1.00 58.16 B O ATOM 3080 N GLN B 391 11.073 9.568 57.553 1.00 59.44 B N ATOM 3081 CA GLN B 391 10.466 9.734 58.868 1.00 57.42 B C ATOM 3082 CB GLN B 391 10.500 8.419 59.651 1.00 58.76 B C ATOM 3083 CG GLN B 391 9.828 7.242 58.956 1.00 59.52 B C ATOM 3084 CD GLN B 391 10.305 5.906 59.504 1.00 60.24 B C ATOM 3085 OE1 GLN B 391 11.045 5.857 60.492 1.00 60.63 B O ATOM 3086 NE2 GLN B 391 9.886 4.814 58.863 1.00 60.01 B N ATOM 3087 C GLN B 391 11.234 10.802 59.624 1.00 56.14 B C ATOM 3088 O GLN B 391 11.093 10.957 60.838 1.00 57.99 B O ATOM 3089 N GLY B 392 12.063 11.538 58.893 1.00 55.06 B N ATOM 3090 CA GLY B 392 12.725 12.696 59.473 1.00 52.23 B C ATOM 3091 C GLY B 392 11.951 13.997 59.302 1.00 48.64 B C ATOM 3092 O GLY B 392 11.120 14.125 58.405 1.00 48.02 B O ATOM 3093 N TYR B 393 12.218 14.962 60.176 1.00 45.86 B N ATOM 3094 CA TYR B 393 11.784 16.326 59.934 1.00 44.61 B C ATOM 3095 CB TYR B 393 11.750 17.145 61.246 1.00 45.06 B C ATOM 3096 CG TYR B 393 10.907 16.536 62.371 1.00 45.65 B C ATOM 3097 CD1 TYR B 393 9.515 16.424 62.256 1.00 45.93 B C ATOM 3098 CE1 TYR B 393 8.752 15.818 63.259 1.00 44.94 B C ATOM 3099 CD2 TYR B 393 11.509 16.031 63.532 1.00 44.52 B C ATOM 3100 CE2 TYR B 393 10.754 15.424 64.533 1.00 43.76 B C ATOM 3101 CZ TYR B 393 9.377 15.318 64.390 1.00 44.07 B C ATOM 3102 OH TYR B 393 8.624 14.691 65.357 1.00 42.13 B O ATOM 3103 C TYR B 393 12.811 16.903 58.955 1.00 44.17 B C ATOM 3104 O TYR B 393 13.982 16.508 58.977 1.00 43.47 B O ATOM 3105 N SER B 394 12.368 17.807 58.081 1.00 42.34 B N ATOM 3106 CA SER B 394 13.252 18.424 57.091 1.00 41.62 B C ATOM 3107 CB SER B 394 12.421 18.988 55.919 1.00 42.32 B C ATOM 3108 OG SER B 394 13.201 19.732 54.983 1.00 38.26 B O ATOM 3109 C SER B 394 14.021 19.543 57.772 1.00 41.53 B C ATOM 3110 O SER B 394 13.432 20.539 58.208 1.00 42.13 B O ATOM 3111 N LEU B 395 15.334 19.382 57.876 1.00 41.12 B N ATOM 3112 CA LEU B 395 16.147 20.402 58.527 1.00 40.33 B C ATOM 3113 CB LEU B 395 17.585 19.907 58.715 1.00 39.97 B C ATOM 3114 CG LEU B 395 18.648 20.950 59.054 1.00 39.72 B C ATOM 3115 CD1 LEU B 395 18.241 21.741 60.268 1.00 38.53 B C ATOM 3116 CD2 LEU B 395 19.986 20.245 59.278 1.00 40.49 B C ATOM 3117 C LEU B 395 16.121 21.661 57.676 1.00 38.64 B C ATOM 3118 O LEU B 395 16.325 22.764 58.173 1.00 39.14 B O ATOM 3119 N PHE B 396 15.842 21.498 56.390 1.00 37.85 B N ATOM 3120 CA PHE B 396 15.764 22.651 55.498 1.00 37.23 B C ATOM 3121 CB PHE B 396 15.773 22.182 54.036 1.00 36.26 B C ATOM 3122 CG PHE B 396 15.257 23.208 53.066 1.00 35.23 B C ATOM 3123 CD1 PHE B 396 15.938 24.401 52.866 1.00 35.91 B C ATOM 3124 CD2 PHE B 396 14.078 22.984 52.373 1.00 34.75 B C ATOM 3125 CE1 PHE B 396 15.454 25.349 52.000 1.00 37.25 B C ATOM 3126 CE2 PHE B 396 13.590 23.924 51.507 1.00 36.35 B C ATOM 3127 CZ PHE B 396 14.277 25.117 51.316 1.00 37.39 B C ATOM 3128 C PHE B 396 14.517 23.497 55.781 1.00 35.29 B C ATOM 3129 O PHE B 396 14.613 24.705 55.900 1.00 33.37 B O ATOM 3130 N LEU B 397 13.363 22.839 55.875 1.00 36.13 B N ATOM 3131 CA LEU B 397 12.102 23.475 56.215 1.00 35.65 B C ATOM 3132 CB LEU B 397 10.958 22.451 56.112 1.00 35.58 B C ATOM 3133 CG LEU B 397 10.473 22.032 54.717 1.00 33.31 B C ATOM 3134 CD1 LEU B 397 9.276 21.108 54.811 1.00 29.11 B C ATOM 3135 CD2 LEU B 397 10.115 23.268 53.932 1.00 32.98 B C ATOM 3136 C LEU B 397 12.107 24.123 57.617 1.00 36.85 B C ATOM 3137 O LEU B 397 11.841 25.323 57.749 1.00 38.10 B O ATOM 3138 N VAL B 398 12.408 23.343 58.658 1.00 36.57 B N ATOM 3139 CA VAL B 398 12.544 23.893 60.016 1.00 35.45 B C ATOM 3140 CB VAL B 398 13.014 22.817 61.039 1.00 34.25 B C ATOM 3141 CG1 VAL B 398 13.410 23.481 62.342 1.00 33.37 B C ATOM 3142 CG2 VAL B 398 11.900 21.820 61.297 1.00 31.49 B C ATOM 3143 C VAL B 398 13.496 25.094 60.091 1.00 35.83 B C ATOM 3144 O VAL B 398 13.177 26.080 60.752 1.00 37.16 B O ATOM 3145 N ALA B 399 14.643 25.029 59.414 1.00 34.37 B N ATOM 3146 CA ALA B 399 15.609 26.130 59.467 1.00 34.75 B C ATOM 3147 CB ALA B 399 16.924 25.726 58.814 1.00 32.68 B C ATOM 3148 C ALA B 399 15.075 27.397 58.808 1.00 35.42 B C ATOM 3149 O ALA B 399 15.168 28.487 59.373 1.00 36.22 B O ATOM 3150 N ALA B 400 14.506 27.246 57.616 1.00 36.86 B N ATOM 3151 CA ALA B 400 13.953 28.374 56.869 1.00 36.50 B C ATOM 3152 CB ALA B 400 13.720 27.992 55.441 1.00 35.95 B C ATOM 3153 C ALA B 400 12.659 28.844 57.499 1.00 38.11 B C ATOM 3154 O ALA B 400 11.953 29.679 56.947 1.00 38.84 B O ATOM 3155 N HIS B 401 12.347 28.299 58.665 1.00 40.38 B N ATOM 3156 CA HIS B 401 11.249 28.822 59.463 1.00 39.90 B C ATOM 3157 CB HIS B 401 10.449 27.689 60.060 1.00 39.12 B C ATOM 3158 CG HIS B 401 9.433 28.134 61.056 1.00 38.70 B C ATOM 3159 CD2 HIS B 401 9.498 28.262 62.401 1.00 38.50 B C ATOM 3160 ND1 HIS B 401 8.143 28.463 60.699 1.00 38.17 B N ATOM 3161 CE1 HIS B 401 7.456 28.771 61.784 1.00 38.22 B C ATOM 3162 NE2 HIS B 401 8.255 28.655 62.830 1.00 37.46 B N ATOM 3163 C HIS B 401 11.808 29.658 60.586 1.00 40.09 B C ATOM 3164 O HIS B 401 11.367 30.791 60.817 1.00 39.85 B O ATOM 3165 N GLU B 402 12.777 29.084 61.290 1.00 38.99 B N ATOM 3166 CA GLU B 402 13.382 29.749 62.436 1.00 40.24 B C ATOM 3167 CB GLU B 402 14.317 28.790 63.209 1.00 42.12 B C ATOM 3168 CG GLU B 402 13.709 27.437 63.658 1.00 43.49 B C ATOM 3169 CD GLU B 402 12.629 27.563 64.746 1.00 44.10 B C ATOM 3170 OE1 GLU B 402 11.993 28.641 64.878 1.00 44.47 B O ATOM 3171 OE2 GLU B 402 12.415 26.567 65.471 1.00 43.52 B O ATOM 3172 C GLU B 402 14.186 30.929 61.937 1.00 39.71 B C ATOM 3173 O GLU B 402 14.435 31.875 62.687 1.00 39.05 B O ATOM 3174 N PHE B 403 14.600 30.851 60.670 1.00 38.09 B N ATOM 3175 CA PHE B 403 15.400 31.895 60.027 1.00 36.23 B C ATOM 3176 CB PHE B 403 15.928 31.398 58.685 1.00 37.44 B C ATOM 3177 CG PHE B 403 17.169 30.572 58.796 1.00 38.52 B C ATOM 3178 CD1 PHE B 403 17.716 30.296 60.034 1.00 38.45 B C ATOM 3179 CD2 PHE B 403 17.792 30.076 57.660 1.00 39.02 B C ATOM 3180 CE1 PHE B 403 18.869 29.529 60.143 1.00 41.58 B C ATOM 3181 CE2 PHE B 403 18.949 29.307 57.756 1.00 41.27 B C ATOM 3182 CZ PHE B 403 19.492 29.031 58.997 1.00 41.84 B C ATOM 3183 C PHE B 403 14.548 33.119 59.802 1.00 36.17 B C ATOM 3184 O PHE B 403 15.058 34.219 59.624 1.00 35.80 B O ATOM 3185 N GLY B 404 13.236 32.908 59.797 1.00 38.73 B N ATOM 3186 CA GLY B 404 12.310 34.020 59.755 1.00 38.07 B C ATOM 3187 C GLY B 404 12.253 34.707 61.100 1.00 38.39 B C ATOM 3188 O GLY B 404 12.197 35.932 61.172 1.00 39.00 B O ATOM 3189 N HIS B 405 12.275 33.926 62.175 1.00 38.03 B N ATOM 3190 CA HIS B 405 12.199 34.514 63.504 1.00 36.49 B C ATOM 3191 CB HIS B 405 12.159 33.436 64.591 1.00 35.77 B C ATOM 3192 CG HIS B 405 10.821 32.784 64.763 1.00 35.75 B C ATOM 3193 CD2 HIS B 405 10.480 31.499 65.025 1.00 34.81 B C ATOM 3194 ND1 HIS B 405 9.639 33.490 64.707 1.00 35.73 B N ATOM 3195 CE1 HIS B 405 8.627 32.670 64.930 1.00 34.91 B C ATOM 3196 NE2 HIS B 405 9.111 31.457 65.125 1.00 34.25 B N ATOM 3197 C HIS B 405 13.448 35.345 63.668 1.00 36.30 B C ATOM 3198 O HIS B 405 13.403 36.423 64.256 1.00 37.02 B O ATOM 3199 N ALA B 406 14.554 34.826 63.131 1.00 35.46 B N ATOM 3200 CA ALA B 406 15.878 35.409 63.313 1.00 34.36 B C ATOM 3201 CB ALA B 406 16.944 34.429 62.852 1.00 33.78 B C ATOM 3202 C ALA B 406 15.983 36.701 62.526 1.00 33.76 B C ATOM 3203 O ALA B 406 16.986 37.412 62.598 1.00 33.68 B O ATOM 3204 N LEU B 407 14.933 37.004 61.775 1.00 35.53 B N ATOM 3205 CA LEU B 407 14.878 38.249 61.020 1.00 37.10 B C ATOM 3206 CB LEU B 407 14.484 37.984 59.563 1.00 37.14 B C ATOM 3207 CG LEU B 407 15.480 37.229 58.680 1.00 37.76 B C ATOM 3208 CD1 LEU B 407 15.079 37.383 57.211 1.00 35.92 B C ATOM 3209 CD2 LEU B 407 16.875 37.778 58.922 1.00 37.13 B C ATOM 3210 C LEU B 407 13.890 39.235 61.623 1.00 37.69 B C ATOM 3211 O LEU B 407 13.910 40.406 61.274 1.00 38.30 B O ATOM 3212 N GLY B 408 13.026 38.763 62.519 1.00 37.38 B N ATOM 3213 CA GLY B 408 12.012 39.642 63.082 1.00 38.09 B C ATOM 3214 C GLY B 408 10.558 39.216 62.882 1.00 37.69 B C ATOM 3215 O GLY B 408 9.632 40.014 63.050 1.00 36.71 B O ATOM 3216 N LEU B 409 10.349 37.954 62.540 1.00 37.60 B N ATOM 3217 CA LEU B 409 9.016 37.498 62.209 1.00 38.95 B C ATOM 3218 CB LEU B 409 9.050 36.615 60.959 1.00 39.90 B C ATOM 3219 CG LEU B 409 9.482 37.357 59.687 1.00 39.78 B C ATOM 3220 CD1 LEU B 409 9.922 36.343 58.682 1.00 39.89 B C ATOM 3221 CD2 LEU B 409 8.359 38.243 59.148 1.00 36.86 B C ATOM 3222 C LEU B 409 8.352 36.751 63.348 1.00 39.36 B C ATOM 3223 O LEU B 409 9.001 36.023 64.096 1.00 39.60 B O ATOM 3224 N ASP B 410 7.043 36.972 63.469 1.00 41.86 B N ATOM 3225 CA ASP B 410 6.167 36.259 64.401 1.00 42.77 B C ATOM 3226 CB ASP B 410 5.061 37.187 64.879 1.00 46.54 B C ATOM 3227 CG ASP B 410 5.392 37.837 66.185 1.00 51.71 B C ATOM 3228 OD1 ASP B 410 6.083 37.159 66.994 1.00 53.97 B O ATOM 3229 OD2 ASP B 410 4.963 39.014 66.404 1.00 53.93 B O ATOM 3230 C ASP B 410 5.530 35.049 63.759 1.00 41.80 B C ATOM 3231 O ASP B 410 5.751 34.762 62.592 1.00 42.23 B O ATOM 3232 N HIS B 411 4.709 34.349 64.516 1.00 40.00 B N ATOM 3233 CA HIS B 411 3.974 33.251 63.928 1.00 41.44 B C ATOM 3234 CB HIS B 411 3.489 32.309 65.029 1.00 41.80 B C ATOM 3235 CG HIS B 411 4.542 31.352 65.492 1.00 41.57 B C ATOM 3236 CD2 HIS B 411 5.474 30.654 64.799 1.00 40.83 B C ATOM 3237 ND1 HIS B 411 4.743 31.050 66.821 1.00 41.15 B N ATOM 3238 CE1 HIS B 411 5.756 30.205 66.926 1.00 41.26 B C ATOM 3239 NE2 HIS B 411 6.216 29.950 65.715 1.00 39.79 B N ATOM 3240 C HIS B 411 2.809 33.677 63.016 1.00 41.49 B C ATOM 3241 O HIS B 411 2.488 34.853 62.909 1.00 42.10 B O ATOM 3242 N SER B 412 2.202 32.707 62.340 1.00 42.34 B N ATOM 3243 CA SER B 412 1.137 32.966 61.381 1.00 42.56 B C ATOM 3244 CB SER B 412 1.636 32.628 59.963 1.00 41.67 B C ATOM 3245 OG SER B 412 0.577 32.533 59.026 1.00 39.29 B O ATOM 3246 C SER B 412 −0.114 32.128 61.734 1.00 43.55 B C ATOM 3247 O SER B 412 −0.019 31.017 62.280 1.00 43.23 B O ATOM 3248 N SER B 413 −1.289 32.668 61.423 1.00 42.94 B N ATOM 3249 CA SER B 413 −2.522 31.942 61.641 1.00 41.70 B C ATOM 3250 CB SER B 413 −3.663 32.903 61.856 1.00 39.34 B C ATOM 3251 OG SER B 413 −3.512 33.523 63.104 1.00 36.89 B O ATOM 3252 C SER B 413 −2.814 31.071 60.455 1.00 44.76 B C ATOM 3253 O SER B 413 −3.429 30.013 60.591 1.00 48.13 B O ATOM 3254 N VAL B 414 −2.373 31.523 59.283 1.00 46.09 B N ATOM 3255 CA VAL B 414 −2.557 30.769 58.053 1.00 45.07 B C ATOM 3256 CB VAL B 414 −1.994 31.512 56.849 1.00 43.16 B C ATOM 3257 CG1 VAL B 414 −2.035 30.603 55.630 1.00 42.06 B C ATOM 3258 CG2 VAL B 414 −2.782 32.769 56.618 1.00 39.39 B C ATOM 3259 C VAL B 414 −1.843 29.443 58.164 1.00 45.83 B C ATOM 3260 O VAL B 414 −0.625 29.386 58.324 1.00 48.07 B O ATOM 3261 N PRO B 415 −2.599 28.348 58.101 1.00 45.54 B N ATOM 3262 CD PRO B 415 −4.068 28.298 58.112 1.00 45.41 B C ATOM 3263 CA PRO B 415 −2.003 27.028 58.319 1.00 46.74 B C ATOM 3264 CB PRO B 415 −3.192 26.080 58.210 1.00 44.77 B C ATOM 3265 CG PRO B 415 −4.345 26.933 58.671 1.00 45.49 B C ATOM 3266 C PRO B 415 −0.898 26.689 57.338 1.00 46.87 B C ATOM 3267 O PRO B 415 0.059 25.992 57.690 1.00 47.32 B O ATOM 3268 N GLU B 416 −1.021 27.184 56.110 1.00 46.57 B N ATOM 3269 CA GLU B 416 −0.177 26.682 55.030 1.00 47.52 B C ATOM 3270 CB GLU B 416 −0.982 26.450 53.753 1.00 50.88 B C ATOM 3271 CG GLU B 416 −2.084 27.477 53.529 1.00 55.90 B C ATOM 3272 CD GLU B 416 −3.283 27.255 54.442 1.00 55.98 B C ATOM 3273 OE1 GLU B 416 −3.408 26.121 54.982 1.00 58.26 B O ATOM 3274 OE2 GLU B 416 −4.088 28.206 54.612 1.00 56.24 B O ATOM 3275 C GLU B 416 0.963 27.612 54.748 1.00 45.16 B C ATOM 3276 O GLU B 416 1.859 27.282 53.971 1.00 45.99 B O ATOM 3277 N ALA B 417 0.948 28.771 55.394 1.00 42.47 B N ATOM 3278 CA ALA B 417 2.106 29.655 55.347 1.00 39.34 B C ATOM 3279 CB ALA B 417 1.781 30.973 56.039 1.00 39.49 B C ATOM 3280 C ALA B 417 3.288 28.970 56.023 1.00 37.24 B C ATOM 3281 O ALA B 417 3.112 28.084 56.851 1.00 35.98 B O ATOM 3282 N LEU B 418 4.491 29.386 55.641 1.00 37.53 B N ATOM 3283 CA LEU B 418 5.736 28.846 56.192 1.00 37.45 B C ATOM 3284 CB LEU B 418 6.929 29.491 55.489 1.00 34.04 B C ATOM 3285 CG LEU B 418 8.221 29.452 56.291 1.00 34.17 B C ATOM 3286 CD1 LEU B 418 8.663 28.014 56.446 1.00 34.24 B C ATOM 3287 CD2 LEU B 418 9.284 30.283 55.621 1.00 32.08 B C ATOM 3288 C LEU B 418 5.854 29.079 57.708 1.00 39.55 B C ATOM 3289 O LEU B 418 6.279 28.196 58.463 1.00 38.65 B O ATOM 3290 N MET B 419 5.480 30.285 58.132 1.00 40.95 B N ATOM 3291 CA MET B 419 5.600 30.716 59.521 1.00 43.11 B C ATOM 3292 CB MET B 419 5.850 32.219 59.569 1.00 42.55 B C ATOM 3293 CG MET B 419 7.101 32.635 58.841 1.00 42.76 B C ATOM 3294 SD MET B 419 8.597 32.262 59.783 1.00 41.81 B S ATOM 3295 CE MET B 419 8.084 32.797 61.378 1.00 41.82 B C ATOM 3296 C MET B 419 4.378 30.370 60.391 1.00 44.74 B C ATOM 3297 O MET B 419 4.127 31.032 61.394 1.00 45.93 B O ATOM 3298 N TYR B 420 3.619 29.348 59.997 1.00 44.36 B N ATOM 3299 CA TYR B 420 2.710 28.651 60.907 1.00 43.02 B C ATOM 3300 CB TYR B 420 1.887 27.627 60.131 1.00 44.47 B C ATOM 3301 CG TYR B 420 0.668 27.112 60.854 1.00 45.27 B C ATOM 3302 CD1 TYR B 420 −0.445 27.925 61.027 1.00 45.02 B C ATOM 3303 CE1 TYR B 420 −1.572 27.467 61.675 1.00 45.09 B C ATOM 3304 CD2 TYR B 420 0.619 25.813 61.354 1.00 44.86 B C ATOM 3305 CE2 TYR B 420 −0.513 25.346 62.005 1.00 44.84 B C ATOM 3306 CZ TYR B 420 −1.602 26.186 62.161 1.00 45.37 B C ATOM 3307 OH TYR B 420 −2.724 25.761 62.822 1.00 46.41 B O ATOM 3308 C TYR B 420 3.585 27.929 61.918 1.00 41.28 B C ATOM 3309 O TYR B 420 4.591 27.342 61.557 1.00 40.84 B O ATOM 3310 N PRO B 421 3.214 27.972 63.205 1.00 41.13 B N ATOM 3311 CD PRO B 421 2.037 28.685 63.739 1.00 40.73 B C ATOM 3312 CA PRO B 421 4.030 27.369 64.276 1.00 42.31 B C ATOM 3313 CB PRO B 421 3.344 27.838 65.567 1.00 39.38 B C ATOM 3314 CG PRO B 421 1.965 28.205 65.171 1.00 39.38 B C ATOM 3315 C PRO B 421 4.178 25.847 64.220 1.00 42.81 B C ATOM 3316 O PRO B 421 4.953 25.260 64.975 1.00 41.12 B O ATOM 3317 N MET B 422 3.442 25.213 63.313 1.00 44.16 B N ATOM 3318 CA MET B 422 3.293 23.756 63.339 1.00 47.55 B C ATOM 3319 CB MET B 422 1.818 23.413 63.392 1.00 50.08 B C ATOM 3320 CG MET B 422 1.469 22.267 64.297 1.00 51.22 B C ATOM 3321 SD MET B 422 −0.240 22.505 64.750 1.00 54.14 B S ATOM 3322 CE MET B 422 −0.021 23.424 66.264 1.00 51.99 B C ATOM 3323 C MET B 422 3.906 23.068 62.126 1.00 47.80 B C ATOM 3324 O MET B 422 3.647 23.467 60.997 1.00 50.19 B O ATOM 3325 N TYR B 423 4.691 22.019 62.343 1.00 48.30 B N ATOM 3326 CA TYR B 423 5.393 21.384 61.231 1.00 46.72 B C ATOM 3327 CB TYR B 423 6.378 20.348 61.739 1.00 43.78 B C ATOM 3328 CG TYR B 423 7.074 19.604 60.635 1.00 41.33 B C ATOM 3329 CD1 TYR B 423 6.433 18.602 59.941 1.00 40.57 B C ATOM 3330 CE1 TYR B 423 7.086 17.882 58.969 1.00 42.30 B C ATOM 3331 CD2 TYR B 423 8.393 19.875 60.321 1.00 40.44 B C ATOM 3332 CE2 TYR B 423 9.061 19.158 59.347 1.00 42.17 B C ATOM 3333 CZ TYR B 423 8.402 18.151 58.673 1.00 42.31 B C ATOM 3334 OH TYR B 423 9.064 17.366 57.745 1.00 42.36 B O ATOM 3335 C TYR B 423 4.485 20.716 60.213 1.00 48.86 B C ATOM 3336 O TYR B 423 3.702 19.827 60.546 1.00 49.99 B O ATOM 3337 N ARG B 424 4.615 21.128 58.959 1.00 50.79 B N ATOM 3338 CA ARG B 424 4.068 20.346 57.856 1.00 51.55 B C ATOM 3339 CB ARG B 424 2.796 20.998 57.304 1.00 53.44 B C ATOM 3340 CG ARG B 424 1.794 19.993 56.722 1.00 56.55 B C ATOM 3341 CD ARG B 424 1.514 18.812 57.673 1.00 59.43 B C ATOM 3342 NE ARG B 424 1.031 19.228 58.997 1.00 61.75 B N ATOM 3343 CZ ARG B 424 0.013 18.661 59.648 1.00 62.85 B C ATOM 3344 NH1 ARG B 424 −0.650 17.645 59.109 1.00 64.88 B N ATOM 3345 NH2 ARG B 424 −0.346 19.112 60.842 1.00 61.29 B N ATOM 3346 C ARG B 424 5.103 20.220 56.755 1.00 49.31 B C ATOM 3347 O ARG B 424 5.635 21.220 56.289 1.00 49.65 B O ATOM 3348 N PHE B 425 5.388 18.984 56.360 1.00 48.81 B N ATOM 3349 CA PHE B 425 6.248 18.719 55.218 1.00 48.21 B C ATOM 3350 CB PHE B 425 6.653 17.233 55.185 1.00 46.50 B C ATOM 3351 CG PHE B 425 7.528 16.878 54.024 1.00 45.66 B C ATOM 3352 CD1 PHE B 425 8.892 17.117 54.070 1.00 44.90 B C ATOM 3353 CD2 PHE B 425 6.981 16.381 52.853 1.00 45.21 B C ATOM 3354 CE1 PHE B 425 9.698 16.878 52.961 1.00 42.93 B C ATOM 3355 CE2 PHE B 425 7.783 16.140 51.738 1.00 43.79 B C ATOM 3356 CZ PHE B 425 9.141 16.392 51.796 1.00 42.38 B C ATOM 3357 C PHE B 425 5.500 19.088 53.930 1.00 48.36 B C ATOM 3358 O PHE B 425 4.297 18.821 53.804 1.00 48.48 B O ATOM 3359 N THR B 426 6.214 19.731 53.002 1.00 48.10 B N ATOM 3360 CA THR B 426 5.763 19.930 51.619 1.00 46.98 B C ATOM 3361 CB THR B 426 5.228 21.360 51.383 1.00 46.58 B C ATOM 3362 OG1 THR B 426 6.262 22.318 51.654 1.00 43.73 B O ATOM 3363 CG2 THR B 426 4.028 21.640 52.273 1.00 45.59 B C ATOM 3364 C THR B 426 6.922 19.701 50.649 1.00 47.26 B C ATOM 3365 O THR B 426 8.078 19.578 51.059 1.00 48.31 B O ATOM 3366 N GLU B 427 6.618 19.638 49.359 1.00 49.22 B N ATOM 3367 CA GLU B 427 7.677 19.620 48.351 1.00 49.60 B C ATOM 3368 CB GLU B 427 7.545 18.378 47.455 1.00 51.62 B C ATOM 3369 CG GLU B 427 7.546 17.039 48.208 1.00 54.42 B C ATOM 3370 CD GLU B 427 8.922 16.385 48.335 1.00 56.16 B C ATOM 3371 OE1 GLU B 427 9.766 16.918 49.087 1.00 57.67 B O ATOM 3372 OE2 GLU B 427 9.155 15.330 47.695 1.00 56.41 B O ATOM 3373 C GLU B 427 7.592 20.903 47.521 1.00 49.73 B C ATOM 3374 O GLU B 427 8.525 21.268 46.789 1.00 48.93 B O ATOM 3375 N GLY B 428 6.463 21.589 47.667 1.00 48.23 B N ATOM 3376 CA GLY B 428 6.252 22.833 46.962 1.00 47.39 B C ATOM 3377 C GLY B 428 7.173 23.918 47.478 1.00 47.18 B C ATOM 3378 O GLY B 428 7.890 23.712 48.474 1.00 48.18 B O ATOM 3379 N PRO B 429 7.185 25.089 46.811 1.00 45.73 B N ATOM 3380 CD PRO B 429 6.567 25.277 45.485 1.00 43.52 B C ATOM 3381 CA PRO B 429 7.883 26.301 47.272 1.00 42.96 B C ATOM 3382 CB PRO B 429 7.508 27.339 46.218 1.00 41.89 B C ATOM 3383 CG PRO B 429 7.208 26.523 44.994 1.00 42.80 B C ATOM 3384 C PRO B 429 7.460 26.726 48.688 1.00 41.18 B C ATOM 3385 O PRO B 429 6.287 27.031 48.930 1.00 40.84 B O ATOM 3386 N PRO B 430 8.414 26.752 49.633 1.00 38.62 B N ATOM 3387 CD PRO B 430 9.845 26.536 49.390 1.00 37.43 B C ATOM 3388 CA PRO B 430 8.127 26.962 51.052 1.00 38.33 B C ATOM 3389 CB PRO B 430 9.490 26.884 51.717 1.00 38.36 B C ATOM 3390 CG PRO B 430 10.354 26.157 50.729 1.00 37.82 B C ATOM 3391 C PRO B 430 7.446 28.280 51.361 1.00 39.82 B C ATOM 3392 O PRO B 430 6.697 28.359 52.315 1.00 41.50 B O ATOM 3393 N LEU B 431 7.713 29.323 50.580 1.00 41.49 B N ATOM 3394 CA LEU B 431 7.182 30.660 50.872 1.00 41.20 B C ATOM 3395 CB LEU B 431 8.052 31.735 50.222 1.00 41.28 B C ATOM 3396 CG LEU B 431 9.244 32.297 50.996 1.00 41.59 B C ATOM 3397 CD1 LEU B 431 9.893 33.397 50.177 1.00 41.94 B C ATOM 3398 CD2 LEU B 431 8.785 32.854 52.337 1.00 41.92 B C ATOM 3399 C LEU B 431 5.757 30.875 50.403 1.00 41.77 B C ATOM 3400 O LEU B 431 5.380 30.454 49.307 1.00 43.80 B O ATOM 3401 N HIS B 432 4.974 31.567 51.224 1.00 42.91 B N ATOM 3402 CA HIS B 432 3.638 32.014 50.825 1.00 42.55 B C ATOM 3403 CB HIS B 432 2.586 31.296 51.659 1.00 44.07 B C ATOM 3404 CG HIS B 432 2.554 29.822 51.426 1.00 45.33 B C ATOM 3405 CD2 HIS B 432 1.622 29.031 50.846 1.00 46.03 B C ATOM 3406 ND1 HIS B 432 3.604 28.999 51.764 1.00 46.05 B N ATOM 3407 CE1 HIS B 432 3.322 27.761 51.399 1.00 45.57 B C ATOM 3408 NE2 HIS B 432 2.126 27.753 50.839 1.00 46.60 B N ATOM 3409 C HIS B 432 3.443 33.514 50.960 1.00 41.63 B C ATOM 3410 O HIS B 432 4.303 34.222 51.489 1.00 40.80 B O ATOM 3411 N LYS B 433 2.296 33.992 50.484 1.00 41.62 B N ATOM 3412 CA LYS B 433 2.013 35.429 50.480 1.00 41.87 B C ATOM 3413 CB LYS B 433 0.588 35.710 49.969 1.00 41.51 B C ATOM 3414 CG LYS B 433 0.378 35.422 48.491 1.00 41.14 B C ATOM 3415 CD LYS B 433 −1.031 35.778 48.017 1.00 40.10 B C ATOM 3416 CE LYS B 433 −1.329 35.169 46.632 1.00 39.04 B C ATOM 3417 NZ LYS B 433 −1.514 36.171 45.540 1.00 37.46 B N ATOM 3418 C LYS B 433 2.170 36.008 51.881 1.00 41.45 B C ATOM 3419 O LYS B 433 2.827 37.038 52.075 1.00 40.46 B O ATOM 3420 N ASP B 434 1.580 35.326 52.857 1.00 42.17 B N ATOM 3421 CA ASP B 434 1.585 35.796 54.243 1.00 43.34 B C ATOM 3422 CB ASP B 434 0.827 34.802 55.135 1.00 45.45 B C ATOM 3423 CG ASP B 434 0.357 35.425 56.429 1.00 48.43 B C ATOM 3424 OD1 ASP B 434 0.014 36.639 56.435 1.00 49.73 B O ATOM 3425 OD2 ASP B 434 0.327 34.704 57.450 1.00 50.16 B O ATOM 3426 C ASP B 434 3.012 35.990 54.769 1.00 42.84 B C ATOM 3427 O ASP B 434 3.309 37.000 55.393 1.00 42.51 B O ATOM 3428 N ASP B 435 3.887 35.022 54.499 1.00 43.41 B N ATOM 3429 CA ASP B 435 5.293 35.103 54.897 1.00 41.10 B C ATOM 3430 CB ASP B 435 6.019 33.827 54.495 1.00 41.22 B C ATOM 3431 CG ASP B 435 5.259 32.583 54.897 1.00 42.48 B C ATOM 3432 OD1 ASP B 435 4.820 32.506 56.073 1.00 41.48 B O ATOM 3433 OD2 ASP B 435 5.105 31.686 54.039 1.00 42.11 B O ATOM 3434 C ASP B 435 6.007 36.293 54.276 1.00 41.27 B C ATOM 3435 O ASP B 435 6.922 36.853 54.881 1.00 41.88 B O ATOM 3436 N VAL B 436 5.601 36.664 53.062 1.00 41.22 B N ATOM 3437 CA VAL B 436 6.276 37.719 52.286 1.00 40.06 B C ATOM 3438 CB VAL B 436 5.978 37.561 50.744 1.00 40.46 B C ATOM 3439 CG1 VAL B 436 6.850 38.511 49.925 1.00 38.14 B C ATOM 3440 CG2 VAL B 436 6.206 36.116 50.311 1.00 40.30 B C ATOM 3441 C VAL B 436 5.792 39.091 52.768 1.00 40.00 B C ATOM 3442 O VAL B 436 6.590 39.992 53.036 1.00 39.11 B O ATOM 3443 N ASN B 437 4.474 39.224 52.893 1.00 40.26 B N ATOM 3444 CA ASN B 437 3.874 40.419 53.488 1.00 40.91 B C ATOM 3445 CB ASN B 437 2.360 40.224 53.679 1.00 40.47 B C ATOM 3446 CG ASN B 437 1.615 40.011 52.353 1.00 42.55 B C ATOM 3447 OD1 ASN B 437 2.021 40.523 51.305 1.00 39.43 B O ATOM 3448 ND2 ASN B 437 0.513 39.247 52.404 1.00 44.70 B N ATOM 3449 C ASN B 437 4.542 40.694 54.835 1.00 39.96 B C ATOM 3450 O ASN B 437 4.910 41.829 55.144 1.00 39.69 B O ATOM 3451 N GLY B 438 4.703 39.639 55.620 1.00 38.71 B N ATOM 3452 CA GLY B 438 5.215 39.805 56.952 1.00 38.08 B C ATOM 3453 C GLY B 438 6.547 40.484 56.865 1.00 38.65 B C ATOM 3454 O GLY B 438 6.814 41.458 57.573 1.00 39.81 B O ATOM 3455 N ILE B 439 7.384 39.980 55.970 1.00 38.30 B N ATOM 3456 CA ILE B 439 8.783 40.352 55.971 1.00 37.86 B C ATOM 3457 CB ILE B 439 9.644 39.291 55.249 1.00 37.09 B C ATOM 3458 CG2 ILE B 439 9.522 39.465 53.762 1.00 37.08 B C ATOM 3459 CG1 ILE B 439 11.116 39.431 55.654 1.00 36.30 B C ATOM 3460 CD1 ILE B 439 11.429 38.993 57.077 1.00 35.31 B C ATOM 3461 C ILE B 439 8.912 41.685 55.264 1.00 38.23 B C ATOM 3462 O ILE B 439 9.743 42.503 55.627 1.00 38.46 B O ATOM 3463 N ARG B 440 8.087 41.919 54.256 1.00 40.44 B N ATOM 3464 CA ARG B 440 8.193 43.177 53.549 1.00 42.16 B C ATOM 3465 CB ARG B 440 7.332 43.173 52.284 1.00 42.50 B C ATOM 3466 CG ARG B 440 8.094 42.845 50.995 1.00 44.01 B C ATOM 3467 CD ARG B 440 7.147 42.525 49.842 1.00 45.03 B C ATOM 3468 NE ARG B 440 7.892 42.116 48.652 1.00 44.27 B N ATOM 3469 CZ ARG B 440 7.355 41.879 47.460 1.00 44.07 B C ATOM 3470 NH1 ARG B 440 6.045 41.999 47.263 1.00 41.72 B N ATOM 3471 NH2 ARG B 440 8.148 41.535 46.458 1.00 41.34 B N ATOM 3472 C ARG B 440 7.736 44.263 54.490 1.00 42.91 B C ATOM 3473 O ARG B 440 8.082 45.422 54.316 1.00 44.99 B O ATOM 3474 N HIS B 441 6.957 43.890 55.498 1.00 45.56 B N ATOM 3475 CA HIS B 441 6.543 44.860 56.501 1.00 46.08 B C ATOM 3476 CB HIS B 441 5.364 44.325 57.330 1.00 48.10 B C ATOM 3477 CG HIS B 441 4.987 45.210 58.482 1.00 50.89 B C ATOM 3478 CD2 HIS B 441 3.859 45.921 58.729 1.00 51.69 B C ATOM 3479 ND1 HIS B 441 5.846 45.482 59.528 1.00 50.80 B N ATOM 3480 CE1 HIS B 441 5.267 46.326 60.364 1.00 50.74 B C ATOM 3481 NE2 HIS B 441 4.061 46.609 59.902 1.00 51.91 B N ATOM 3482 C HIS B 441 7.719 45.191 57.421 1.00 45.64 B C ATOM 3483 O HIS B 441 7.747 46.245 58.038 1.00 46.37 B O ATOM 3484 N LEU B 442 8.692 44.297 57.525 1.00 46.18 B N ATOM 3485 CA LEU B 442 9.865 44.605 58.328 1.00 46.63 B C ATOM 3486 CB LEU B 442 10.508 43.325 58.837 1.00 45.09 B C ATOM 3487 CG LEU B 442 9.675 42.675 59.926 1.00 44.22 B C ATOM 3488 CD1 LEU B 442 9.929 41.190 59.944 1.00 46.17 B C ATOM 3489 CD2 LEU B 442 10.005 43.316 61.252 1.00 44.60 B C ATOM 3490 C LEU B 442 10.900 45.421 57.577 1.00 46.92 B C ATOM 3491 O LEU B 442 11.390 46.431 58.082 1.00 48.54 B O ATOM 3492 N TYR B 443 11.222 44.986 56.365 1.00 46.18 B N ATOM 3493 CA TYR B 443 12.377 45.501 55.657 1.00 45.03 B C ATOM 3494 CB TYR B 443 13.332 44.347 55.321 1.00 44.32 B C ATOM 3495 CG TYR B 443 13.878 43.642 56.550 1.00 42.42 B C ATOM 3496 CD1 TYR B 443 13.424 42.373 56.912 1.00 40.39 B C ATOM 3497 CE1 TYR B 443 13.880 41.760 58.051 1.00 40.28 B C ATOM 3498 CD2 TYR B 443 14.815 44.273 57.372 1.00 40.30 B C ATOM 3499 CE2 TYR B 443 15.279 43.676 58.513 1.00 40.12 B C ATOM 3500 CZ TYR B 443 14.808 42.420 58.854 1.00 41.05 B C ATOM 3501 OH TYR B 443 15.245 41.832 60.027 1.00 42.54 B O ATOM 3502 C TYR B 443 11.986 46.242 54.389 1.00 45.86 B C ATOM 3503 O TYR B 443 12.793 46.977 53.818 1.00 46.88 B O ATOM 3504 N GLY B 444 10.752 46.043 53.941 1.00 46.03 B N ATOM 3505 CA GLY B 444 10.288 46.729 52.750 1.00 45.07 B C ATOM 3506 C GLY B 444 10.067 45.826 51.559 1.00 45.52 B C ATOM 3507 O GLY B 444 9.299 46.176 50.662 1.00 45.69 B O ATOM 3508 ZN ZN B 500 8.315 29.493 65.204 1.00 35.51 B ZN ATOM 3509 ZN ZN B 501 18.046 27.204 72.671 1.00 46.18 B ZN ATOM 3510 CA CA B 502 11.649 17.628 70.817 1.00 47.54 B CA ATOM 3512 CA CA B 504 23.285 36.518 67.728 1.00 67.08 B CA TER 3513 CA B 504 B ATOM 3514 C1 INH R 1 10.624 34.268 74.963 1.00 70.23 A996 C ATOM 3515 O2 INH R 1 10.379 33.340 73.866 1.00 70.69 A996 O ATOM 3516 C3 INH R 1 11.393 32.717 73.262 1.00 70.19 A996 C ATOM 3517 C4 INH R 1 11.867 31.470 73.736 1.00 70.00 A996 C ATOM 3518 C5 INH R 1 12.946 30.835 73.081 1.00 69.99 A996 C ATOM 3519 C6 INH R 1 13.551 31.439 71.963 1.00 71.13 A996 C ATOM 3520 C7 INH R 1 13.076 32.686 71.488 1.00 71.11 A996 C ATOM 3521 C8 INH R 1 11.995 33.317 72.144 1.00 69.78 A996 C ATOM 3522 N9 INH R 1 11.487 34.500 71.755 1.00 68.26 A996 N ATOM 3523 C10 INH R 1 11.271 35.069 70.580 1.00 68.35 A996 C ATOM 3524 N11 INH R 1 10.757 36.230 70.278 1.00 69.95 A996 N ATOM 3525 C12 INH R 1 10.610 36.638 69.076 1.00 70.47 A996 C ATOM 3526 C13 INH R 1 11.033 35.751 68.036 1.00 68.94 A996 C ATOM 3527 S14 INH R 1 11.620 34.388 68.967 1.00 66.10 A996 S ATOM 3528 C15 INH R 1 10.010 37.982 68.744 1.00 71.40 A996 C ATOM 3529 S16 INH R 1 8.847 38.671 69.857 1.00 71.95 A996 S ATOM 3530 C17 INH R 1 8.573 40.162 68.901 1.00 72.74 A996 C ATOM 3531 N18 INH R 1 9.362 40.000 67.873 1.00 73.50 A996 N ATOM 3532 C19 INH R 1 10.099 38.922 67.755 1.00 72.77 A996 C ATOM 3533 C20 INH R 1 11.074 38.642 66.561 1.00 75.19 A996 C ATOM 3534 N21 INH R 1 7.733 41.028 69.365 1.00 73.74 A996 N ATOM 3535 C22 INH R 1 7.941 42.002 70.266 1.00 75.95 A996 C ATOM 3536 C23 INH R 1 7.893 43.470 69.865 1.00 74.12 A996 C ATOM 3537 O24 INH R 1 8.179 41.677 71.436 1.00 78.08 A996 O TER 3538 INH R 1 A996 END

TABLE 12 Coordinates for pro MMP9(35-444 ΔFnII) (SEQ ID NO: 12) complex with Example 2 ATOM 1 CB ASP A 41 42.276 26.353 −23.632 1.00 56.15 C ATOM 2 CG ASP A 41 42.803 26.503 −22.206 1.00 50.47 C ATOM 3 OD1 ASP A 41 42.470 25.682 −21.319 1.00 47.03 O ATOM 4 OD2 ASP A 41 43.570 27.449 −21.982 1.00 45.65 O ATOM 5 C ASP A 41 40.793 28.391 −23.790 1.00 54.63 C ATOM 6 O ASP A 41 40.058 28.991 −23.000 1.00 50.61 O ATOM 7 N ASP A 41 40.263 26.359 −25.026 1.00 44.97 N ATOM 8 CA ASP A 41 40.844 26.864 −23.792 1.00 52.91 C ATOM 9 N ARG A 42 41.566 29.018 −24.676 1.00 55.47 N ATOM 10 CA ARG A 42 41.378 30.443 −24.971 1.00 58.48 C ATOM 11 CB ARG A 42 42.482 30.990 −25.883 1.00 57.59 C ATOM 12 CG ARG A 42 42.313 32.466 −26.221 1.00 52.05 C ATOM 13 CD ARG A 42 43.192 32.899 −27.398 1.00 59.22 C ATOM 14 NE ARG A 42 43.453 34.343 −27.390 1.00 55.57 N ATOM 15 CZ ARG A 42 42.592 35.269 −27.807 1.00 62.43 C ATOM 16 NH1 ARG A 42 41.400 34.910 −28.294 1.00 53.74 N ATOM 17 NH2 ARG A 42 42.925 36.557 −27.740 1.00 64.55 N ATOM 18 C ARG A 42 40.025 30.666 −25.646 1.00 54.38 C ATOM 19 O ARG A 42 39.562 31.798 −25.739 1.00 47.98 O ATOM 20 N GLN A 43 39.389 29.634 −26.165 1.00 60.65 N ATOM 21 CA GLN A 43 38.064 29.757 −26.734 1.00 57.04 C ATOM 22 CB GLN A 43 37.827 28.639 −27.718 1.00 56.67 C ATOM 23 CG GLN A 43 38.645 28.624 −29.000 1.00 66.89 C ATOM 24 CD GLN A 43 38.123 27.575 −29.986 1.00 70.35 C ATOM 25 OE1 GLN A 43 37.246 27.873 −30.789 1.00 54.17 O ATOM 26 NE2 GLN A 43 38.630 26.351 −29.902 1.00 55.05 N ATOM 27 C GLN A 43 36.991 29.635 −25.677 1.00 57.85 C ATOM 28 O GLN A 43 35.937 30.169 −25.849 1.00 48.29 O ATOM 29 N LEU A 44 37.255 28.856 −24.621 1.00 60.48 N ATOM 30 CA LEU A 44 36.400 28.775 −23.447 1.00 50.39 C ATOM 31 CB LEU A 44 36.960 27.705 −22.510 1.00 44.19 C ATOM 32 CG LEU A 44 36.286 27.347 −21.181 1.00 62.86 C ATOM 33 CD1 LEU A 44 36.859 26.035 −20.627 1.00 62.47 C ATOM 34 CD2 LEU A 44 36.443 28.455 −20.150 1.00 50.97 C ATOM 35 C LEU A 44 36.286 30.121 −22.738 1.00 48.55 C ATOM 36 O LEU A 44 35.241 30.449 −22.188 1.00 50.86 O ATOM 37 N ALA A 45 37.349 30.909 −22.766 1.00 48.16 N ATOM 38 CA ALA A 45 37.357 32.184 −22.062 1.00 48.97 C ATOM 39 CB ALA A 45 38.768 32.635 −21.805 1.00 48.86 C ATOM 40 C ALA A 45 36.644 33.214 −22.896 1.00 49.69 C ATOM 41 O ALA A 45 36.076 34.173 −22.389 1.00 53.64 O ATOM 42 N GLU A 46 36.692 33.017 −24.198 1.00 50.58 N ATOM 43 CA GLU A 46 36.048 33.941 −25.095 1.00 54.09 C ATOM 44 CB GLU A 46 36.589 33.717 −26.512 1.00 58.02 C ATOM 45 CG GLU A 46 36.014 34.627 −27.554 1.00 67.50 C ATOM 46 CD GLU A 46 34.615 34.224 −27.919 1.00 68.42 C ATOM 47 OE1 GLU A 46 34.399 33.031 −28.214 1.00 70.96 O ATOM 48 OE2 GLU A 46 33.728 35.094 −27.886 1.00 70.00 O ATOM 49 C GLU A 46 34.525 33.745 −24.950 1.00 53.11 C ATOM 50 O GLU A 46 33.777 34.703 −24.719 1.00 48.28 O ATOM 51 N GLU A 47 34.090 32.490 −25.038 1.00 51.62 N ATOM 52 CA GLU A 47 32.707 32.090 −24.762 1.00 51.50 C ATOM 53 CB GLU A 47 32.580 30.564 −24.906 1.00 52.04 C ATOM 54 CG GLU A 47 31.789 29.849 −23.808 1.00 55.06 C ATOM 55 CD GLU A 47 30.304 29.730 −24.120 1.00 59.81 C ATOM 56 OE1 GLU A 47 29.954 29.385 −25.273 1.00 67.96 O ATOM 57 OE2 GLU A 47 29.488 29.973 −23.208 1.00 58.49 O ATOM 58 C GLU A 47 32.204 32.554 −23.379 1.00 53.40 C ATOM 59 O GLU A 47 31.130 33.171 −23.268 1.00 46.34 O ATOM 60 N TYR A 48 32.990 32.254 −22.343 1.00 45.68 N ATOM 61 CA TYR A 48 32.674 32.638 −20.977 1.00 40.55 C ATOM 62 CB TYR A 48 33.824 32.221 −20.042 1.00 41.85 C ATOM 63 CG TYR A 48 33.554 32.352 −18.560 1.00 36.21 C ATOM 64 CD1 TYR A 48 33.767 33.557 −17.893 1.00 39.38 C ATOM 65 CE1 TYR A 48 33.541 33.679 −16.526 1.00 34.44 C ATOM 66 CD2 TYR A 48 33.108 31.270 −17.821 1.00 35.15 C ATOM 67 CE2 TYR A 48 32.876 31.381 −16.441 1.00 35.84 C ATOM 68 CZ TYR A 48 33.092 32.585 −15.805 1.00 33.64 C ATOM 69 OH TYR A 48 32.851 32.704 −14.454 1.00 33.43 O ATOM 70 C TYR A 48 32.486 34.136 −20.906 1.00 38.10 C ATOM 71 O TYR A 48 31.445 34.617 −20.495 1.00 41.53 O ATOM 72 N LEU A 49 33.516 34.870 −21.305 1.00 44.92 N ATOM 73 CA LEU A 49 33.488 36.329 −21.282 1.00 45.61 C ATOM 74 CB LEU A 49 34.752 36.901 −21.932 1.00 40.51 C ATOM 75 CG LEU A 49 36.024 36.932 −21.086 1.00 40.89 C ATOM 76 CD1 LEU A 49 37.222 37.355 −21.932 1.00 46.73 C ATOM 77 CD2 LEU A 49 35.857 37.878 −19.910 1.00 47.61 C ATOM 78 C LEU A 49 32.230 36.940 −21.917 1.00 48.03 C ATOM 79 O LEU A 49 31.664 37.889 −21.373 1.00 53.13 O ATOM 80 N TYR A 50 31.809 36.403 −23.062 1.00 47.81 N ATOM 81 CA TYR A 50 30.587 36.842 −23.737 1.00 52.81 C ATOM 82 CB TYR A 50 30.497 36.221 −25.133 1.00 53.67 C ATOM 83 CG TYR A 50 29.158 36.438 −25.809 1.00 65.03 C ATOM 84 CD1 TYR A 50 28.848 37.661 −26.411 1.00 65.29 C ATOM 85 CE1 TYR A 50 27.621 37.868 −27.034 1.00 62.49 C ATOM 86 CD2 TYR A 50 28.202 35.422 −25.854 1.00 64.43 C ATOM 87 CE2 TYR A 50 26.973 35.619 −26.479 1.00 59.37 C ATOM 88 CZ TYR A 50 26.688 36.844 −27.067 1.00 64.66 C ATOM 89 OH TYR A 50 25.468 37.052 −27.690 1.00 67.01 O ATOM 90 C TYR A 50 29.329 36.482 −22.934 1.00 54.74 C ATOM 91 O TYR A 50 28.572 37.362 −22.497 1.00 54.26 O ATOM 92 N ARG A 51 29.134 35.178 −22.746 1.00 50.49 N ATOM 93 CA ARG A 51 28.027 34.608 −21.986 1.00 46.69 C ATOM 94 CB ARG A 51 28.366 33.163 −21.635 1.00 48.10 C ATOM 95 CG ARG A 51 27.303 32.419 −20.887 1.00 46.09 C ATOM 96 CD ARG A 51 27.692 30.960 −20.761 1.00 46.35 C ATOM 97 NE ARG A 51 26.971 30.092 −21.694 1.00 54.53 N ATOM 98 CZ ARG A 51 25.649 29.904 −21.675 1.00 56.77 C ATOM 99 NH1 ARG A 51 24.903 30.545 −20.782 1.00 59.68 N ATOM 100 NH2 ARG A 51 25.066 29.085 −22.548 1.00 50.23 N ATOM 101 C ARG A 51 27.656 35.384 −20.718 1.00 51.85 C ATOM 102 O ARG A 51 26.521 35.871 −20.608 1.00 42.92 O ATOM 103 N TYR A 52 28.601 35.502 −19.775 1.00 43.77 N ATOM 104 CA TYR A 52 28.342 36.197 −18.505 1.00 42.06 C ATOM 105 CB TYR A 52 29.169 35.602 −17.352 1.00 43.74 C ATOM 106 CG TYR A 52 28.937 34.109 −17.256 1.00 46.12 C ATOM 107 CD1 TYR A 52 29.836 33.215 −17.823 1.00 44.19 C ATOM 108 CE1 TYR A 52 29.609 31.850 −17.787 1.00 40.96 C ATOM 109 CD2 TYR A 52 27.772 33.591 −16.673 1.00 42.36 C ATOM 110 CE2 TYR A 52 27.537 32.224 −16.631 1.00 39.48 C ATOM 111 CZ TYR A 52 28.472 31.362 −17.201 1.00 42.45 C ATOM 112 OH TYR A 52 28.294 30.002 −17.200 1.00 46.29 O ATOM 113 C TYR A 52 28.494 37.707 −18.618 1.00 47.87 C ATOM 114 O TYR A 52 28.609 38.418 −17.618 1.00 51.07 O ATOM 115 N GLY A 53 28.485 38.186 −19.856 1.00 47.98 N ATOM 116 CA GLY A 53 28.323 39.597 −20.145 1.00 52.80 C ATOM 117 C GLY A 53 29.533 40.498 −20.004 1.00 58.35 C ATOM 118 O GLY A 53 29.370 41.703 −19.815 1.00 58.84 O ATOM 119 N TYR A 54 30.740 39.945 −20.123 1.00 52.60 N ATOM 120 CA TYR A 54 31.941 40.741 −19.884 1.00 51.98 C ATOM 121 CB TYR A 54 33.050 39.903 −19.244 1.00 53.02 C ATOM 122 CG TYR A 54 32.808 39.518 −17.789 1.00 53.03 C ATOM 123 CD1 TYR A 54 32.262 38.283 −17.454 1.00 47.86 C ATOM 124 CE1 TYR A 54 32.066 37.924 −16.137 1.00 50.84 C ATOM 125 CD2 TYR A 54 33.154 40.377 −16.755 1.00 54.20 C ATOM 126 CE2 TYR A 54 32.941 40.033 −15.434 1.00 50.67 C ATOM 127 CZ TYR A 54 32.408 38.805 −15.133 1.00 50.09 C ATOM 128 OH TYR A 54 32.207 38.459 −13.824 1.00 52.44 O ATOM 129 C TYR A 54 32.464 41.463 −21.130 1.00 58.22 C ATOM 130 O TYR A 54 33.103 42.522 −21.032 1.00 58.02 O ATOM 131 N THR A 55 32.211 40.924 −22.313 1.00 57.96 N ATOM 132 CA THR A 55 32.713 41.636 −23.483 1.00 57.85 C ATOM 133 CB THR A 55 32.602 40.788 −24.721 1.00 51.99 C ATOM 134 OG1 THR A 55 31.245 40.792 −25.158 1.00 57.89 O ATOM 135 CG2 THR A 55 33.036 39.356 −24.389 1.00 45.18 C ATOM 136 C THR A 55 32.061 43.049 −23.622 1.00 62.84 C ATOM 137 O THR A 55 30.824 43.205 −23.594 1.00 53.73 O ATOM 138 O ALA A 56 34.917 46.072 −23.270 1.00 53.72 O ATOM 139 N ALA A 56 32.939 44.053 −23.742 1.00 63.37 N ATOM 140 CA ALA A 56 32.661 45.472 −23.500 1.00 62.65 C ATOM 141 C ALA A 56 33.898 46.252 −23.918 1.00 55.47 C ATOM 142 CB ALA A 56 32.419 45.703 −21.996 1.00 50.66 C ATOM 143 O ALA A 57 31.201 48.765 −24.400 1.00 50.51 O ATOM 144 N ALA A 57 33.864 47.138 −24.924 1.00 47.35 N ATOM 145 CA ALA A 57 32.743 47.472 −25.843 1.00 51.42 C ATOM 146 C ALA A 57 31.789 48.658 −25.493 1.00 50.81 C ATOM 147 CB ALA A 57 31.981 46.225 −26.304 1.00 51.59 C ATOM 148 N LEU A 67 41.431 41.501 −25.811 1.00 50.48 N ATOM 149 CA LEU A 67 40.825 40.408 −25.059 1.00 49.24 C ATOM 150 CB LEU A 67 41.313 39.066 −25.619 1.00 52.47 C ATOM 151 CG LEU A 67 40.611 37.752 −25.252 1.00 51.62 C ATOM 152 CD1 LEU A 67 41.093 37.224 −23.911 1.00 53.59 C ATOM 153 CD2 LEU A 67 39.104 37.905 −25.270 1.00 42.29 C ATOM 154 C LEU A 67 41.135 40.526 −23.553 1.00 52.25 C ATOM 155 O LEU A 67 40.495 39.889 −22.719 1.00 51.49 O ATOM 156 N GLY A 68 42.108 41.355 −23.207 1.00 44.21 N ATOM 157 CA GLY A 68 42.499 41.492 −21.817 1.00 51.82 C ATOM 158 C GLY A 68 41.699 42.482 −20.978 1.00 49.01 C ATOM 159 O GLY A 68 41.576 42.332 −19.758 1.00 46.88 O ATOM 160 N PRO A 69 41.173 43.526 −21.615 1.00 48.90 N ATOM 161 CD PRO A 69 41.370 44.024 −22.990 1.00 50.41 C ATOM 162 CA PRO A 69 40.419 44.461 −20.790 1.00 41.43 C ATOM 163 CB PRO A 69 40.065 45.579 −21.770 1.00 46.02 C ATOM 164 CG PRO A 69 41.121 45.494 −22.838 1.00 52.10 C ATOM 165 C PRO A 69 39.175 43.784 −20.216 1.00 50.73 C ATOM 166 O PRO A 69 38.725 44.144 −19.111 1.00 55.70 O ATOM 167 N ALA A 70 38.647 42.797 −20.938 1.00 48.84 N ATOM 168 CA ALA A 70 37.525 41.983 −20.449 1.00 46.83 C ATOM 169 CB ALA A 70 36.891 41.183 −21.592 1.00 42.15 C ATOM 170 C ALA A 70 37.973 41.038 −19.343 1.00 44.77 C ATOM 171 O ALA A 70 37.242 40.785 −18.399 1.00 41.81 O ATOM 172 N LEU A 71 39.175 40.496 −19.481 1.00 49.85 N ATOM 173 CA LEU A 71 39.723 39.629 −18.448 1.00 48.87 C ATOM 174 CB LEU A 71 41.056 39.026 −18.885 1.00 45.26 C ATOM 175 CG LEU A 71 40.989 37.851 −19.854 1.00 45.37 C ATOM 176 CD1 LEU A 71 42.400 37.365 −20.197 1.00 46.93 C ATOM 177 CD2 LEU A 71 40.150 36.735 −19.279 1.00 32.21 C ATOM 178 C LEU A 71 39.919 40.408 −17.155 1.00 45.54 C ATOM 179 O LEU A 71 39.809 39.853 −16.065 1.00 46.62 O ATOM 180 N LEU A 72 40.207 41.694 −17.281 1.00 45.20 N ATOM 181 CA LEU A 72 40.512 42.504 −16.115 1.00 46.18 C ATOM 182 CB LEU A 72 41.199 43.787 −16.553 1.00 51.43 C ATOM 183 CG LEU A 72 42.266 44.410 −15.660 1.00 59.35 C ATOM 184 CD1 LEU A 72 43.328 43.388 −15.238 1.00 55.19 C ATOM 185 CD2 LEU A 72 42.896 45.591 −16.382 1.00 50.31 C ATOM 186 C LEU A 72 39.186 42.799 −15.433 1.00 50.47 C ATOM 187 O LEU A 72 39.066 42.742 −14.204 1.00 54.25 O ATOM 188 N LEU A 73 38.185 43.089 −16.257 1.00 49.79 N ATOM 189 CA LEU A 73 36.799 43.246 −15.817 1.00 47.42 C ATOM 190 CB LEU A 73 35.893 43.391 −17.047 1.00 48.53 C ATOM 191 CG LEU A 73 35.894 44.754 −17.717 1.00 49.08 C ATOM 192 CD1 LEU A 73 34.906 44.755 −18.874 1.00 43.60 C ATOM 193 CD2 LEU A 73 35.559 45.820 −16.669 1.00 33.83 C ATOM 194 C LEU A 73 36.316 42.040 −15.038 1.00 44.79 C ATOM 195 O LEU A 73 35.661 42.164 −14.006 1.00 40.16 O ATOM 196 N LEU A 74 36.604 40.872 −15.597 1.00 48.28 N ATOM 197 CA LEU A 74 36.196 39.614 −15.028 1.00 46.79 C ATOM 198 CB LEU A 74 36.563 38.469 −15.958 1.00 47.70 C ATOM 199 CG LEU A 74 36.593 37.086 −15.310 1.00 46.82 C ATOM 200 CD1 LEU A 74 35.348 36.898 −14.484 1.00 57.65 C ATOM 201 CD2 LEU A 74 36.671 36.009 −16.377 1.00 48.43 C ATOM 202 C LEU A 74 36.910 39.442 −13.722 1.00 49.49 C ATOM 203 O LEU A 74 36.323 38.996 −12.742 1.00 47.78 O ATOM 204 N GLN A 75 38.182 39.812 −13.703 1.00 45.60 N ATOM 205 CA GLN A 75 38.980 39.565 −12.520 1.00 42.88 C ATOM 206 CB GLN A 75 40.461 39.761 −12.820 1.00 42.13 C ATOM 207 CG GLN A 75 40.980 38.701 −13.768 1.00 45.31 C ATOM 208 CD GLN A 75 42.396 38.949 −14.260 1.00 47.87 C ATOM 209 OE1 GLN A 75 42.849 40.092 −14.379 1.00 47.74 O ATOM 210 NE2 GLN A 75 43.095 37.869 −14.557 1.00 44.05 N ATOM 211 C GLN A 75 38.503 40.411 −11.358 1.00 45.35 C ATOM 212 O GLN A 75 38.478 39.951 −10.213 1.00 44.47 O ATOM 213 N LYS A 76 38.098 41.640 −11.654 1.00 48.78 N ATOM 214 CA LYS A 76 37.544 42.501 −10.618 1.00 52.94 C ATOM 215 CB LYS A 76 37.239 43.899 −11.157 1.00 52.22 C ATOM 216 CG LYS A 76 38.457 44.656 −11.646 1.00 56.96 C ATOM 217 CD LYS A 76 39.165 45.386 −10.509 1.00 59.79 C ATOM 218 CE LYS A 76 40.449 46.038 −11.002 1.00 58.27 C ATOM 219 NZ LYS A 76 40.377 46.234 −12.481 1.00 56.38 N ATOM 220 C LYS A 76 36.268 41.860 −10.104 1.00 50.11 C ATOM 221 O LYS A 76 36.130 41.593 −8.919 1.00 55.41 O ATOM 222 N GLN A 77 35.344 41.601 −11.013 1.00 46.14 N ATOM 223 CA GLN A 77 34.047 41.050 −10.649 1.00 48.65 C ATOM 224 CB GLN A 77 33.248 40.705 −11.913 1.00 50.45 C ATOM 225 CG GLN A 77 31.825 40.252 −11.641 1.00 55.05 C ATOM 226 CD GLN A 77 31.037 41.306 −10.893 1.00 59.69 C ATOM 227 OE1 GLN A 77 31.208 42.509 −11.138 1.00 65.43 O ATOM 228 NE2 GLN A 77 30.188 40.871 −9.961 1.00 52.87 N ATOM 229 C GLN A 77 34.123 39.828 −9.726 1.00 50.42 C ATOM 230 O GLN A 77 33.234 39.614 −8.888 1.00 52.32 O ATOM 231 N LEU A 78 35.165 39.017 −9.875 1.00 46.29 N ATOM 232 CA LEU A 78 35.248 37.790 −9.080 1.00 49.32 C ATOM 233 CB LEU A 78 35.608 36.597 −9.954 1.00 49.30 C ATOM 234 CG LEU A 78 34.584 36.252 −11.027 1.00 50.88 C ATOM 235 CD1 LEU A 78 34.919 34.924 −11.642 1.00 40.69 C ATOM 236 CD2 LEU A 78 33.197 36.222 −10.391 1.00 52.27 C ATOM 237 C LEU A 78 36.237 37.912 −7.931 1.00 51.33 C ATOM 238 O LEU A 78 36.388 36.991 −7.121 1.00 46.25 O ATOM 239 N SER A 79 36.910 39.057 −7.864 1.00 55.21 N ATOM 240 CA SER A 79 37.895 39.300 −6.820 1.00 46.54 C ATOM 241 CB SER A 79 37.287 39.051 −5.438 1.00 48.23 C ATOM 242 OG SER A 79 36.149 39.870 −5.230 1.00 45.62 O ATOM 243 C SER A 79 39.058 38.364 −7.046 1.00 43.75 C ATOM 244 O SER A 79 39.441 37.623 −6.154 1.00 48.33 O ATOM 245 N LEU A 80 39.571 38.351 −8.268 1.00 46.43 N ATOM 246 CA LEU A 80 40.758 37.584 −8.589 1.00 44.62 C ATOM 247 CB LEU A 80 40.558 36.764 −9.869 1.00 42.78 C ATOM 248 CG LEU A 80 39.411 35.738 −9.924 1.00 44.28 C ATOM 249 CD1 LEU A 80 39.186 35.209 −11.343 1.00 45.45 C ATOM 250 CD2 LEU A 80 39.648 34.574 −8.985 1.00 43.56 C ATOM 251 C LEU A 80 41.860 38.620 −8.769 1.00 45.84 C ATOM 252 O LEU A 80 41.572 39.817 −8.872 1.00 41.52 O ATOM 253 N PRO A 81 43.127 38.179 −8.766 1.00 42.24 N ATOM 254 CD PRO A 81 43.703 36.902 −8.305 1.00 41.32 C ATOM 255 CA PRO A 81 44.151 39.186 −9.040 1.00 45.24 C ATOM 256 CB PRO A 81 45.456 38.387 −8.992 1.00 45.38 C ATOM 257 CG PRO A 81 45.168 37.251 −8.041 1.00 43.68 C ATOM 258 C PRO A 81 43.900 39.779 −10.415 1.00 47.46 C ATOM 259 O PRO A 81 43.649 39.043 −11.373 1.00 49.07 O ATOM 260 N GLU A 82 43.952 41.105 −10.494 1.00 48.97 N ATOM 261 CA GLU A 82 43.652 41.834 −11.728 1.00 54.87 C ATOM 262 CB GLU A 82 43.154 43.246 −11.385 1.00 51.05 C ATOM 263 CG GLU A 82 41.723 43.252 −10.916 1.00 51.92 C ATOM 264 CD GLU A 82 41.585 43.503 −9.435 1.00 60.23 C ATOM 265 OE1 GLU A 82 40.438 43.499 −8.931 1.00 57.29 O ATOM 266 OE2 GLU A 82 42.624 43.702 −8.767 1.00 73.34 O ATOM 267 C GLU A 82 44.814 41.871 −12.733 1.00 49.48 C ATOM 268 O GLU A 82 45.359 42.935 −13.042 1.00 52.18 O ATOM 269 N THR A 83 45.173 40.702 −13.256 1.00 51.21 N ATOM 270 CA THR A 83 46.378 40.574 −14.083 1.00 42.40 C ATOM 271 CB THR A 83 46.946 39.157 −14.052 1.00 43.39 C ATOM 272 OG1 THR A 83 46.026 38.262 −14.683 1.00 41.77 O ATOM 273 CG2 THR A 83 47.225 38.707 −12.615 1.00 35.23 C ATOM 274 C THR A 83 46.125 40.930 −15.528 1.00 45.49 C ATOM 275 O THR A 83 47.045 41.320 −16.243 1.00 53.64 O ATOM 276 N GLY A 84 44.883 40.798 −15.973 1.00 44.45 N ATOM 277 CA GLY A 84 44.561 41.158 −17.337 1.00 46.34 C ATOM 278 C GLY A 84 45.161 40.140 −18.268 1.00 49.04 C ATOM 279 O GLY A 84 45.047 40.245 −19.483 1.00 55.46 O ATOM 280 N GLU A 85 45.798 39.139 −17.679 1.00 49.40 N ATOM 281 CA GLU A 85 46.332 38.014 −18.420 1.00 47.91 C ATOM 282 CB GLU A 85 47.777 37.754 −17.993 1.00 50.84 C ATOM 283 CG GLU A 85 48.709 37.452 −19.157 1.00 60.46 C ATOM 284 CD GLU A 85 49.177 38.710 −19.866 1.00 59.52 C ATOM 285 OE1 GLU A 85 49.412 38.654 −21.098 1.00 71.10 O ATOM 286 OE2 GLU A 85 49.308 39.752 −19.186 1.00 58.26 O ATOM 287 C GLU A 85 45.475 36.792 −18.112 1.00 52.94 C ATOM 288 O GLU A 85 44.944 36.668 −16.996 1.00 51.20 O ATOM 289 N LEU A 86 45.330 35.892 −19.088 1.00 53.71 N ATOM 290 CA LEU A 86 44.615 34.635 −18.861 1.00 45.10 C ATOM 291 CB LEU A 86 44.094 34.036 −20.168 1.00 41.02 C ATOM 292 CG LEU A 86 43.395 32.680 −20.026 1.00 42.08 C ATOM 293 CD1 LEU A 86 42.171 32.782 −19.134 1.00 44.13 C ATOM 294 CD2 LEU A 86 43.009 32.104 −21.378 1.00 38.66 C ATOM 295 C LEU A 86 45.523 33.642 −18.135 1.00 45.66 C ATOM 296 O LEU A 86 46.212 32.835 −18.761 1.00 48.83 O ATOM 297 N ASP A 87 45.499 33.708 −16.808 1.00 44.76 N ATOM 298 CA ASP A 87 46.417 32.964 −15.952 1.00 43.31 C ATOM 299 CB ASP A 87 46.990 33.892 −14.872 1.00 40.58 C ATOM 300 CG ASP A 87 45.903 34.734 −14.183 1.00 46.62 C ATOM 301 OD1 ASP A 87 44.792 34.189 −13.973 1.00 47.61 O ATOM 302 OD2 ASP A 87 46.157 35.930 −13.859 1.00 35.47 O ATOM 303 C ASP A 87 45.738 31.772 −15.300 1.00 42.01 C ATOM 304 O ASP A 87 44.688 31.307 −15.751 1.00 43.57 O ATOM 305 N SER A 88 46.330 31.282 −14.223 1.00 36.92 N ATOM 306 CA SER A 88 45.838 30.057 −13.611 1.00 42.88 C ATOM 307 CB SER A 88 46.944 29.313 −12.862 1.00 42.49 C ATOM 308 OG SER A 88 47.471 28.286 −13.691 1.00 45.31 O ATOM 309 C SER A 88 44.644 30.293 −12.714 1.00 39.25 C ATOM 310 O SER A 88 43.713 29.494 −12.681 1.00 43.63 O ATOM 311 N ALA A 89 44.659 31.389 −11.983 1.00 42.63 N ATOM 312 CA ALA A 89 43.492 31.718 −11.189 1.00 38.69 C ATOM 313 CB ALA A 89 43.718 32.981 −10.433 1.00 35.53 C ATOM 314 C ALA A 89 42.353 31.886 −12.173 1.00 41.99 C ATOM 315 O ALA A 89 41.343 31.201 −12.090 1.00 45.73 O ATOM 316 N THR A 90 42.537 32.786 −13.131 1.00 41.39 N ATOM 317 CA THR A 90 41.489 33.069 −14.095 1.00 42.56 C ATOM 318 CB THR A 90 41.940 34.084 −15.151 1.00 40.77 C ATOM 319 OG1 THR A 90 42.141 35.353 −14.512 1.00 38.65 O ATOM 320 CG2 THR A 90 40.893 34.244 −16.217 1.00 35.44 C ATOM 321 C THR A 90 40.942 31.793 −14.729 1.00 42.52 C ATOM 322 O THR A 90 39.752 31.508 −14.588 1.00 44.47 O ATOM 323 N LEU A 91 41.797 31.007 −15.376 1.00 37.83 N ATOM 324 CA LEU A 91 41.316 29.813 −16.082 1.00 44.43 C ATOM 325 CB LEU A 91 42.453 29.070 −16.796 1.00 42.17 C ATOM 326 CG LEU A 91 42.067 27.673 −17.298 1.00 40.90 C ATOM 327 CD1 LEU A 91 41.115 27.764 −18.474 1.00 44.17 C ATOM 328 CD2 LEU A 91 43.288 26.844 −17.672 1.00 39.48 C ATOM 329 C LEU A 91 40.591 28.849 −15.156 1.00 42.26 C ATOM 330 O LEU A 91 39.640 28.168 −15.562 1.00 43.65 O ATOM 331 N LYS A 92 41.058 28.771 −13.919 1.00 38.49 N ATOM 332 CA LYS A 92 40.490 27.827 −12.971 1.00 40.03 C ATOM 333 CB LYS A 92 41.364 27.743 −11.714 1.00 43.16 C ATOM 334 CG LYS A 92 40.718 27.075 −10.489 1.00 47.06 C ATOM 335 CD LYS A 92 41.191 27.751 −9.207 1.00 47.31 C ATOM 336 CE LYS A 92 40.335 27.373 −8.002 1.00 61.33 C ATOM 337 NZ LYS A 92 40.604 25.978 −7.546 1.00 65.27 N ATOM 338 C LYS A 92 39.077 28.283 −12.624 1.00 45.13 C ATOM 339 O LYS A 92 38.138 27.471 −12.580 1.00 42.72 O ATOM 340 N ALA A 93 38.936 29.587 −12.384 1.00 39.88 N ATOM 341 CA ALA A 93 37.633 30.184 −12.157 1.00 35.94 C ATOM 342 CB ALA A 93 37.764 31.672 −11.945 1.00 34.88 C ATOM 343 C ALA A 93 36.688 29.876 −13.323 1.00 40.37 C ATOM 344 O ALA A 93 35.568 29.443 −13.099 1.00 46.23 O ATOM 345 N MET A 94 37.147 30.068 −14.556 1.00 36.12 N ATOM 346 CA MET A 94 36.295 29.866 −15.735 1.00 42.70 C ATOM 347 CB MET A 94 37.002 30.285 −17.039 1.00 42.32 C ATOM 348 CG MET A 94 37.206 31.778 −17.209 1.00 44.94 C ATOM 349 SD MET A 94 37.991 32.191 −18.788 1.00 48.36 S ATOM 350 CE MET A 94 38.485 33.888 −18.502 1.00 36.87 C ATOM 351 C MET A 94 35.851 28.430 −15.876 1.00 40.24 C ATOM 352 O MET A 94 34.840 28.153 −16.530 1.00 41.43 O ATOM 353 N ARG A 95 36.612 27.512 −15.287 1.00 40.36 N ATOM 354 CA ARG A 95 36.301 26.084 −15.399 1.00 41.60 C ATOM 355 CB ARG A 95 37.583 25.247 −15.534 1.00 44.90 C ATOM 356 CG ARG A 95 38.453 25.599 −16.736 1.00 51.62 C ATOM 357 CD ARG A 95 39.062 24.356 −17.390 1.00 52.15 C ATOM 358 NE ARG A 95 40.474 24.148 −17.057 1.00 63.27 N ATOM 359 CZ ARG A 95 41.417 23.817 −17.948 1.00 66.87 C ATOM 360 NH1 ARG A 95 41.097 23.666 −19.232 1.00 58.28 N ATOM 361 NH2 ARG A 95 42.683 23.643 −17.564 1.00 56.25 N ATOM 362 C ARG A 95 35.458 25.569 −14.227 1.00 38.86 C ATOM 363 O ARG A 95 35.278 24.364 −14.065 1.00 40.60 O ATOM 364 N THR A 96 34.952 26.494 −13.416 1.00 46.44 N ATOM 365 CA THR A 96 34.200 26.173 −12.202 1.00 47.00 C ATOM 366 CB THR A 96 34.654 27.089 −11.031 1.00 44.80 C ATOM 367 OG1 THR A 96 35.882 26.603 −10.500 1.00 45.65 O ATOM 368 CG2 THR A 96 33.633 27.117 −9.916 1.00 43.95 C ATOM 369 C THR A 96 32.691 26.330 −12.444 1.00 47.66 C ATOM 370 O THR A 96 32.245 27.372 −12.926 1.00 48.40 O ATOM 371 N PRO A 97 31.902 25.297 −12.112 1.00 48.66 N ATOM 372 CD PRO A 97 32.262 24.034 −11.449 1.00 53.35 C ATOM 373 CA PRO A 97 30.471 25.355 −12.432 1.00 52.48 C ATOM 374 CB PRO A 97 29.932 24.007 −11.930 1.00 51.20 C ATOM 375 CG PRO A 97 31.125 23.118 −11.849 1.00 56.36 C ATOM 376 C PRO A 97 29.824 26.499 −11.688 1.00 46.86 C ATOM 377 O PRO A 97 30.240 26.790 −10.579 1.00 45.12 O ATOM 378 N ARG A 98 28.830 27.138 −12.297 1.00 48.63 N ATOM 379 CA ARG A 98 28.278 28.366 −11.747 1.00 46.36 C ATOM 380 CB ARG A 98 29.136 29.559 −12.171 1.00 47.90 C ATOM 381 CG ARG A 98 29.286 29.693 −13.701 1.00 41.67 C ATOM 382 CD ARG A 98 29.790 31.085 −14.087 1.00 38.11 C ATOM 383 NE ARG A 98 28.752 32.100 −13.901 1.00 38.62 N ATOM 384 CZ ARG A 98 28.989 33.394 −13.688 1.00 42.69 C ATOM 385 NH1 ARG A 98 27.985 34.236 −13.541 1.00 43.15 N ATOM 386 NH2 ARG A 98 30.232 33.854 −13.621 1.00 49.47 N ATOM 387 C ARG A 98 26.862 28.632 −12.199 1.00 42.34 C ATOM 388 O ARG A 98 26.263 27.889 −12.973 1.00 48.21 O ATOM 389 N CYS A 99 26.355 29.751 −11.732 1.00 42.22 N ATOM 390 CA CYS A 99 24.988 30.145 −11.961 1.00 41.05 C ATOM 391 CB CYS A 99 24.590 31.106 −10.846 1.00 38.15 C ATOM 392 SG CYS A 99 23.146 32.072 −11.120 1.00 40.30 S ATOM 393 C CYS A 99 24.922 30.804 −13.323 1.00 42.83 C ATOM 394 O CYS A 99 25.788 31.600 −13.661 1.00 42.16 O ATOM 395 N GLY A 100 23.900 30.465 −14.104 1.00 43.32 N ATOM 396 CA GLY A 100 23.759 30.974 −15.459 1.00 40.61 C ATOM 397 C GLY A 100 23.418 32.450 −15.608 1.00 43.87 C ATOM 398 O GLY A 100 23.334 32.966 −16.722 1.00 51.82 O ATOM 399 N VAL A 101 23.200 33.138 −14.497 1.00 44.50 N ATOM 400 CA VAL A 101 22.865 34.560 −14.536 1.00 43.99 C ATOM 401 CB VAL A 101 22.181 34.992 −13.230 1.00 39.39 C ATOM 402 CG1 VAL A 101 21.917 36.489 −13.216 1.00 45.01 C ATOM 403 CG2 VAL A 101 20.895 34.239 −13.052 1.00 45.33 C ATOM 404 C VAL A 101 24.113 35.410 −14.783 1.00 43.04 C ATOM 405 O VAL A 101 25.158 35.170 −14.186 1.00 44.26 O ATOM 406 N PRO A 102 24.010 36.398 −15.679 1.00 43.05 N ATOM 407 CD PRO A 102 22.833 36.657 −16.526 1.00 47.10 C ATOM 408 CA PRO A 102 25.155 37.235 −16.058 1.00 49.00 C ATOM 409 CB PRO A 102 24.610 38.065 −17.237 1.00 51.38 C ATOM 410 CG PRO A 102 23.426 37.291 −17.744 1.00 46.31 C ATOM 411 C PRO A 102 25.632 38.156 −14.933 1.00 45.19 C ATOM 412 O PRO A 102 24.822 38.654 −14.151 1.00 49.20 O ATOM 413 N ASP A 103 26.933 38.417 −14.900 1.00 49.15 N ATOM 414 CA ASP A 103 27.559 39.173 −13.816 1.00 52.26 C ATOM 415 CB ASP A 103 28.964 38.644 −13.590 1.00 47.96 C ATOM 416 CG ASP A 103 28.975 37.167 −13.403 1.00 48.49 C ATOM 417 OD1 ASP A 103 28.033 36.667 −12.753 1.00 48.84 O ATOM 418 OD2 ASP A 103 29.903 36.507 −13.904 1.00 45.43 O ATOM 419 C ASP A 103 27.641 40.665 −14.082 1.00 53.86 C ATOM 420 O ASP A 103 28.014 41.432 −13.194 1.00 54.69 O ATOM 421 N LEU A 104 27.340 41.064 −15.315 1.00 53.14 N ATOM 422 CA LEU A 104 27.282 42.473 −15.687 1.00 52.80 C ATOM 423 CB LEU A 104 28.643 42.985 −16.157 1.00 54.70 C ATOM 424 CG LEU A 104 29.819 43.106 −15.185 1.00 58.44 C ATOM 425 CD1 LEU A 104 31.122 43.300 −15.925 1.00 54.26 C ATOM 426 CD2 LEU A 104 29.616 44.237 −14.197 1.00 65.64 C ATOM 427 C LEU A 104 26.267 42.623 −16.802 1.00 59.65 C ATOM 428 O LEU A 104 26.575 42.330 −17.965 1.00 48.70 O ATOM 429 N GLY A 105 25.051 43.046 −16.430 1.00 72.75 N ATOM 430 CA GLY A 105 23.947 43.258 −17.361 1.00 62.05 C ATOM 431 C GLY A 105 24.428 43.999 −18.595 1.00 63.30 C ATOM 432 O GLY A 105 25.626 44.201 −18.752 1.00 65.09 O ATOM 433 N ARG A 106 23.532 44.389 −19.473 1.00 65.16 N ATOM 434 CA ARG A 106 22.131 44.290 −19.253 1.00 64.41 C ATOM 435 CB ARG A 106 21.601 45.688 −18.879 1.00 67.33 C ATOM 436 CG ARG A 106 22.057 46.222 −17.443 1.00 70.75 C ATOM 437 CD ARG A 106 22.747 47.660 −17.300 1.00 72.23 C ATOM 438 NE ARG A 106 23.449 48.161 −18.486 1.00 70.98 N ATOM 439 CZ ARG A 106 23.300 49.367 −19.008 1.00 63.39 C ATOM 440 NH1 ARG A 106 23.938 49.687 −20.095 1.00 57.67 N ATOM 441 NH2 ARG A 106 22.497 50.250 −18.463 1.00 66.94 N ATOM 442 C ARG A 106 21.535 43.756 −20.536 1.00 64.99 C ATOM 443 O ARG A 106 20.939 44.493 −21.242 1.00 68.51 O ATOM 444 N PHE A 107 21.735 42.464 −20.822 1.00 67.13 N ATOM 445 CA PHE A 107 21.277 41.753 −22.027 1.00 62.44 C ATOM 446 CB PHE A 107 21.498 40.238 −21.852 1.00 65.46 C ATOM 447 CG PHE A 107 22.903 39.768 −22.184 1.00 76.56 C ATOM 448 CD1 PHE A 107 23.114 38.523 −22.786 1.00 74.75 C ATOM 449 CD2 PHE A 107 24.009 40.566 −21.906 1.00 70.17 C ATOM 450 CE1 PHE A 107 24.399 38.086 −23.101 1.00 67.24 C ATOM 451 CE2 PHE A 107 25.294 40.136 −22.221 1.00 64.72 C ATOM 452 CZ PHE A 107 25.488 38.893 −22.819 1.00 61.90 C ATOM 453 C PHE A 107 19.813 42.009 −22.433 1.00 64.24 C ATOM 454 O PHE A 107 19.531 42.458 −23.538 1.00 65.19 O ATOM 455 N GLN A 108 18.884 41.839 −21.526 1.00 65.81 N ATOM 456 CA GLN A 108 17.505 42.099 −21.856 1.00 62.44 C ATOM 457 CB GLN A 108 16.775 40.779 −22.002 1.00 56.04 C ATOM 458 CG GLN A 108 15.772 40.507 −20.967 1.00 58.40 C ATOM 459 CD GLN A 108 15.921 39.164 −20.399 1.00 56.87 C ATOM 460 OE1 GLN A 108 16.839 38.450 −20.731 1.00 50.61 O ATOM 461 NE2 GLN A 108 15.032 38.801 −19.531 1.00 61.84 N ATOM 462 C GLN A 108 16.795 43.022 −20.867 1.00 66.02 C ATOM 463 O GLN A 108 17.330 43.370 −19.834 1.00 66.14 O ATOM 464 N THR A 109 15.576 43.412 −21.209 1.00 70.09 N ATOM 465 CA THR A 109 14.765 44.299 −20.394 1.00 64.64 C ATOM 466 CB THR A 109 14.199 45.448 −21.247 1.00 64.13 C ATOM 467 OG1 THR A 109 14.890 46.647 −20.934 1.00 74.30 O ATOM 468 CG2 THR A 109 12.773 45.669 −20.966 1.00 62.52 C ATOM 469 C THR A 109 13.646 43.570 −19.649 1.00 58.59 C ATOM 470 O THR A 109 12.999 42.713 −20.188 1.00 56.43 O ATOM 471 N PHE A 110 13.463 43.932 −18.386 1.00 65.55 N ATOM 472 CA PHE A 110 12.364 43.439 −17.546 1.00 55.85 C ATOM 473 CB PHE A 110 12.897 42.806 −16.255 1.00 57.28 C ATOM 474 CG PHE A 110 13.920 41.724 −16.469 1.00 57.21 C ATOM 475 CD1 PHE A 110 15.278 42.019 −16.436 1.00 49.31 C ATOM 476 CD2 PHE A 110 13.525 40.408 −16.681 1.00 53.55 C ATOM 477 CE1 PHE A 110 16.212 41.030 −16.623 1.00 50.76 C ATOM 478 CE2 PHE A 110 14.462 39.409 −16.875 1.00 49.90 C ATOM 479 CZ PHE A 110 15.809 39.719 −16.843 1.00 50.00 C ATOM 480 C PHE A 110 11.413 44.576 −17.166 1.00 57.19 C ATOM 481 O PHE A 110 11.739 45.749 −17.319 1.00 58.76 O ATOM 482 N GLU A 111 10.239 44.225 −16.652 1.00 59.56 N ATOM 483 CA GLU A 111 9.271 45.230 −16.206 1.00 64.27 C ATOM 484 CB GLU A 111 7.842 44.812 −16.564 1.00 67.04 C ATOM 485 CG GLU A 111 7.562 44.650 −18.036 1.00 67.63 C ATOM 486 CD GLU A 111 6.117 44.294 −18.279 1.00 76.56 C ATOM 487 OE1 GLU A 111 5.281 44.656 −17.429 1.00 75.91 O ATOM 488 OE2 GLU A 111 5.814 43.651 −19.307 1.00 89.70 O ATOM 489 C GLU A 111 9.336 45.508 −14.700 1.00 64.45 C ATOM 490 O GLU A 111 9.612 44.615 −13.885 1.00 53.57 O ATOM 491 N GLY A 112 9.058 46.756 −14.338 1.00 64.70 N ATOM 492 CA GLY A 112 8.932 47.110 −12.943 1.00 61.35 C ATOM 493 C GLY A 112 10.265 47.065 −12.239 1.00 62.25 C ATOM 494 O GLY A 112 11.272 46.713 −12.838 1.00 54.45 O ATOM 495 N ASP A 113 10.251 47.391 −10.949 1.00 57.75 N ATOM 496 CA ASP A 113 11.461 47.718 −10.219 1.00 53.51 C ATOM 497 CB ASP A 113 11.123 48.684 −9.076 1.00 60.72 C ATOM 498 CG ASP A 113 10.223 48.053 −8.006 1.00 60.18 C ATOM 499 OD1 ASP A 113 9.528 47.056 −8.296 1.00 54.01 O ATOM 500 OD2 ASP A 113 10.220 48.559 −6.862 1.00 60.39 O ATOM 501 C ASP A 113 12.244 46.512 −9.689 1.00 55.92 C ATOM 502 O ASP A 113 13.122 46.672 −8.838 1.00 57.96 O ATOM 503 N LEU A 114 11.932 45.319 −10.194 1.00 57.92 N ATOM 504 CA LEU A 114 12.630 44.072 −9.811 1.00 60.26 C ATOM 505 CB LEU A 114 14.058 44.030 −10.380 1.00 54.16 C ATOM 506 CG LEU A 114 14.170 44.204 −11.894 1.00 56.72 C ATOM 507 CD1 LEU A 114 15.454 43.573 −12.423 1.00 55.13 C ATOM 508 CD2 LEU A 114 12.962 43.582 −12.572 1.00 58.94 C ATOM 509 C LEU A 114 12.661 43.766 −8.306 1.00 52.92 C ATOM 510 O LEU A 114 13.595 43.139 −7.811 1.00 50.32 O ATOM 511 N LYS A 115 11.630 44.202 −7.593 1.00 57.50 N ATOM 512 CA LYS A 115 11.486 43.925 −6.166 1.00 52.92 C ATOM 513 CB LYS A 115 11.657 45.221 −5.376 1.00 56.69 C ATOM 514 CG LYS A 115 11.810 45.054 −3.881 1.00 54.39 C ATOM 515 CD LYS A 115 12.147 46.384 −3.219 1.00 57.30 C ATOM 516 CE LYS A 115 10.905 47.253 −3.090 1.00 62.66 C ATOM 517 NZ LYS A 115 10.833 47.923 −1.757 1.00 54.06 N ATOM 518 C LYS A 115 10.081 43.391 −5.970 1.00 51.29 C ATOM 519 O LYS A 115 9.166 43.810 −6.676 1.00 53.25 O ATOM 520 N TRP A 116 9.885 42.462 −5.042 1.00 51.25 N ATOM 521 CA TRP A 116 8.521 42.034 −4.749 1.00 48.90 C ATOM 522 CB TRP A 116 8.481 40.707 −4.008 1.00 47.77 C ATOM 523 CG TRP A 116 8.902 39.522 −4.819 1.00 50.21 C ATOM 524 CD2 TRP A 116 8.359 39.096 −6.074 1.00 50.95 C ATOM 525 CE2 TRP A 116 9.049 37.935 −6.454 1.00 50.48 C ATOM 526 CE3 TRP A 116 7.347 39.581 −6.908 1.00 56.19 C ATOM 527 CD1 TRP A 116 9.877 38.627 −4.506 1.00 51.21 C ATOM 528 NE1 TRP A 116 9.973 37.670 −5.481 1.00 50.39 N ATOM 529 CZ2 TRP A 116 8.767 37.254 −7.631 1.00 54.20 C ATOM 530 CZ3 TRP A 116 7.069 38.902 −8.081 1.00 50.06 C ATOM 531 CH2 TRP A 116 7.774 37.753 −8.430 1.00 54.63 C ATOM 532 C TRP A 116 7.827 43.107 −3.926 1.00 54.26 C ATOM 533 O TRP A 116 8.440 43.731 −3.068 1.00 52.01 O ATOM 534 N HIS A 117 6.544 43.328 −4.195 1.00 57.36 N ATOM 535 CA HIS A 117 5.802 44.359 −3.484 1.00 51.37 C ATOM 536 CB HIS A 117 5.376 45.478 −4.436 1.00 53.71 C ATOM 537 CG HIS A 117 6.527 46.265 −4.972 1.00 52.27 C ATOM 538 CD2 HIS A 117 7.487 46.982 −4.339 1.00 54.85 C ATOM 539 ND1 HIS A 117 6.809 46.350 −6.318 1.00 50.63 N ATOM 540 CE1 HIS A 117 7.887 47.094 −6.492 1.00 51.48 C ATOM 541 NE2 HIS A 117 8.323 47.486 −5.307 1.00 51.19 N ATOM 542 C HIS A 117 4.619 43.835 −2.672 1.00 50.90 C ATOM 543 O HIS A 117 3.770 44.622 −2.259 1.00 52.08 O ATOM 544 N HIS A 118 4.563 42.514 −2.469 1.00 49.23 N ATOM 545 CA HIS A 118 3.759 41.906 −1.392 1.00 51.08 C ATOM 546 CB HIS A 118 2.670 40.937 −1.898 1.00 42.24 C ATOM 547 CG HIS A 118 3.122 40.018 −2.991 1.00 51.95 C ATOM 548 CD2 HIS A 118 3.056 38.671 −3.105 1.00 51.19 C ATOM 549 ND1 HIS A 118 3.688 40.474 −4.164 1.00 49.61 N ATOM 550 CE1 HIS A 118 3.978 39.445 −4.940 1.00 53.96 C ATOM 551 NE2 HIS A 118 3.604 38.338 −4.321 1.00 48.37 N ATOM 552 C HIS A 118 4.705 41.226 −0.417 1.00 52.56 C ATOM 553 O HIS A 118 5.912 41.427 −0.496 1.00 58.59 O ATOM 554 N HIS A 119 4.182 40.425 0.499 1.00 50.43 N ATOM 555 CA HIS A 119 5.037 39.887 1.556 1.00 61.41 C ATOM 556 CB HIS A 119 4.831 40.645 2.880 1.00 55.66 C ATOM 557 CG HIS A 119 5.653 41.896 2.984 1.00 53.06 C ATOM 558 CD2 HIS A 119 6.223 42.668 2.029 1.00 54.39 C ATOM 559 ND1 HIS A 119 5.989 42.471 4.192 1.00 60.46 N ATOM 560 CE1 HIS A 119 6.725 43.549 3.976 1.00 57.96 C ATOM 561 NE2 HIS A 119 6.884 43.689 2.672 1.00 62.70 N ATOM 562 C HIS A 119 4.936 38.378 1.739 1.00 58.18 C ATOM 563 O HIS A 119 5.818 37.750 2.339 1.00 55.13 O ATOM 564 N ASN A 120 3.871 37.798 1.206 1.00 55.11 N ATOM 565 CA ASN A 120 3.793 36.352 1.120 1.00 52.35 C ATOM 566 CB ASN A 120 2.450 35.825 1.601 1.00 60.37 C ATOM 567 CG ASN A 120 2.417 34.314 1.637 1.00 61.21 C ATOM 568 OD1 ASN A 120 3.472 33.662 1.601 1.00 51.04 O ATOM 569 ND2 ASN A 120 1.208 33.743 1.701 1.00 60.23 N ATOM 570 C ASN A 120 4.024 35.906 −0.298 1.00 53.76 C ATOM 571 O ASN A 120 3.088 35.780 −1.086 1.00 49.50 O ATOM 572 N ILE A 121 5.294 35.690 −0.600 1.00 54.06 N ATOM 573 CA ILE A 121 5.752 35.208 −1.883 1.00 47.54 C ATOM 574 CB ILE A 121 7.274 35.255 −1.921 1.00 49.06 C ATOM 575 CG2 ILE A 121 7.794 34.367 −3.012 1.00 55.34 C ATOM 576 CG1 ILE A 121 7.761 36.684 −2.153 1.00 51.75 C ATOM 577 CD1 ILE A 121 7.224 37.679 −1.182 1.00 54.18 C ATOM 578 C ILE A 121 5.291 33.769 −2.100 1.00 50.94 C ATOM 579 O ILE A 121 5.475 32.924 −1.223 1.00 51.60 O ATOM 580 N THR A 122 4.690 33.488 −3.262 1.00 49.74 N ATOM 581 CA THR A 122 4.093 32.175 −3.500 1.00 51.71 C ATOM 582 CB THR A 122 2.632 32.282 −4.033 1.00 51.20 C ATOM 583 OG1 THR A 122 2.643 32.547 −5.434 1.00 52.96 O ATOM 584 CG2 THR A 122 1.881 33.401 −3.343 1.00 54.13 C ATOM 585 C THR A 122 4.929 31.398 −4.494 1.00 45.98 C ATOM 586 O THR A 122 5.441 31.974 −5.445 1.00 49.02 O ATOM 587 N TYR A 123 5.070 30.094 −4.283 1.00 44.26 N ATOM 588 CA TYR A 123 5.886 29.286 −5.187 1.00 46.58 C ATOM 589 CB TYR A 123 7.326 29.176 −4.680 1.00 49.58 C ATOM 590 CG TYR A 123 7.525 28.290 −3.469 1.00 46.90 C ATOM 591 CD1 TYR A 123 7.638 28.838 −2.203 1.00 47.55 C ATOM 592 CE1 TYR A 123 7.842 28.041 −1.089 1.00 50.74 C ATOM 593 CD2 TYR A 123 7.632 26.912 −3.597 1.00 47.13 C ATOM 594 CE2 TYR A 123 7.827 26.100 −2.489 1.00 50.65 C ATOM 595 CZ TYR A 123 7.931 26.674 −1.236 1.00 52.18 C ATOM 596 OH TYR A 123 8.138 25.895 −0.127 1.00 40.34 O ATOM 597 C TYR A 123 5.321 27.896 −5.473 1.00 55.80 C ATOM 598 O TYR A 123 4.635 27.296 −4.640 1.00 60.09 O ATOM 599 N TRP A 124 5.629 27.389 −6.662 1.00 52.93 N ATOM 600 CA TRP A 124 5.097 26.126 −7.147 1.00 53.19 C ATOM 601 CB TRP A 124 4.119 26.426 −8.293 1.00 61.88 C ATOM 602 CG TRP A 124 3.491 25.242 −9.004 1.00 56.85 C ATOM 603 CD2 TRP A 124 3.178 25.167 −10.393 1.00 54.75 C ATOM 604 CE2 TRP A 124 2.589 23.906 −10.623 1.00 56.63 C ATOM 605 CE3 TRP A 124 3.351 26.041 −11.474 1.00 57.81 C ATOM 606 CD1 TRP A 124 3.082 24.059 −8.453 1.00 58.27 C ATOM 607 NE1 TRP A 124 2.549 23.245 −9.425 1.00 56.38 N ATOM 608 CZ2 TRP A 124 2.172 23.498 −11.888 1.00 54.12 C ATOM 609 CZ3 TRP A 124 2.932 25.641 −12.725 1.00 60.01 C ATOM 610 CH2 TRP A 124 2.354 24.373 −12.924 1.00 61.31 C ATOM 611 C TRP A 124 6.266 25.287 −7.641 1.00 56.70 C ATOM 612 O TRP A 124 7.090 25.760 −8.423 1.00 54.36 O ATOM 613 N ILE A 125 6.352 24.048 −7.178 1.00 55.69 N ATOM 614 CA ILE A 125 7.392 23.148 −7.657 1.00 46.99 C ATOM 615 CB ILE A 125 7.750 22.096 −6.575 1.00 51.68 C ATOM 616 CG2 ILE A 125 8.874 21.162 −7.040 1.00 48.21 C ATOM 617 CG1 ILE A 125 8.103 22.792 −5.249 1.00 53.66 C ATOM 618 CD1 ILE A 125 8.335 21.833 −4.073 1.00 49.89 C ATOM 619 C ILE A 125 6.908 22.489 −8.944 1.00 49.22 C ATOM 620 O ILE A 125 6.578 21.310 −8.951 1.00 54.48 O ATOM 621 N GLN A 126 6.855 23.270 −10.024 1.00 48.65 N ATOM 622 CA GLN A 126 6.315 22.836 −11.319 1.00 50.25 C ATOM 623 CB GLN A 126 6.691 23.830 −12.424 1.00 51.85 C ATOM 624 CG GLN A 126 6.292 23.387 −13.842 1.00 50.44 C ATOM 625 CD GLN A 126 6.339 24.538 −14.855 1.00 56.36 C ATOM 626 OE1 GLN A 126 7.253 24.626 −15.685 1.00 57.60 O ATOM 627 NE2 GLN A 126 5.351 25.427 −14.784 1.00 52.75 N ATOM 628 C GLN A 126 6.692 21.418 −11.767 1.00 51.12 C ATOM 629 O GLN A 126 5.941 20.774 −12.496 1.00 52.04 O ATOM 630 N ASN A 127 7.859 20.945 −11.355 1.00 52.03 N ATOM 631 CA ASN A 127 8.276 19.584 −11.670 1.00 52.89 C ATOM 632 CB ASN A 127 8.531 19.401 −13.172 1.00 55.37 C ATOM 633 CG ASN A 127 9.537 20.391 −13.733 1.00 54.56 C ATOM 634 OD1 ASN A 127 9.732 21.478 −13.192 0.47 55.18 O ATOM 635 ND2 ASN A 127 10.175 20.019 −14.836 1.00 56.55 N ATOM 636 C ASN A 127 9.487 19.157 −10.852 0.65 55.64 C ATOM 637 O ASN A 127 10.063 19.970 −10.124 1.00 55.14 O ATOM 638 N TYR A 128 9.860 17.885 −10.980 1.00 53.40 N ATOM 639 CA TYR A 128 10.940 17.307 −10.189 1.00 55.06 C ATOM 640 CB TYR A 128 10.379 16.241 −9.247 1.00 55.84 C ATOM 641 CG TYR A 128 9.488 16.809 −8.155 1.00 63.24 C ATOM 642 CD1 TYR A 128 9.992 17.072 −6.884 1.00 61.81 C ATOM 643 CE1 TYR A 128 9.189 17.588 −5.892 1.00 60.10 C ATOM 644 CD2 TYR A 128 8.148 17.086 −8.400 1.00 58.51 C ATOM 645 CE2 TYR A 128 7.343 17.601 −7.419 1.00 61.09 C ATOM 646 CZ TYR A 128 7.866 17.854 −6.163 1.00 62.92 C ATOM 647 OH TYR A 128 7.052 18.372 −5.181 1.00 62.43 O ATOM 648 C TYR A 128 12.102 16.711 −10.997 1.00 60.61 C ATOM 649 O TYR A 128 11.926 16.247 −12.116 1.00 57.50 O ATOM 650 N SER A 129 13.296 16.742 −10.416 1.00 63.01 N ATOM 651 CA SER A 129 14.400 15.948 −10.918 1.00 56.03 C ATOM 652 CB SER A 129 15.734 16.489 −10.400 1.00 59.89 C ATOM 653 OG SER A 129 16.839 15.849 −11.022 1.00 61.43 O ATOM 654 C SER A 129 14.148 14.558 −10.374 1.00 61.89 C ATOM 655 O SER A 129 13.574 14.407 −9.296 1.00 67.24 O ATOM 656 N GLU A 130 14.546 13.540 −11.123 1.00 66.36 N ATOM 657 CA GLU A 130 14.322 12.171 −10.683 1.00 69.32 C ATOM 658 CB GLU A 130 14.110 11.237 −11.875 1.00 72.68 C ATOM 659 CG GLU A 130 12.643 10.895 −12.113 1.00 80.39 C ATOM 660 CD GLU A 130 11.925 10.456 −10.831 1.00 84.49 C ATOM 661 OE1 GLU A 130 11.990 9.252 −10.484 1.00 88.58 O ATOM 662 OE2 GLU A 130 11.301 11.319 −10.169 1.00 79.70 O ATOM 663 C GLU A 130 15.491 11.719 −9.847 1.00 63.71 C ATOM 664 O GLU A 130 15.492 10.618 −9.291 1.00 62.78 O ATOM 665 N ASP A 131 16.487 12.594 −9.770 1.00 65.00 N ATOM 666 CA ASP A 131 17.679 12.362 −8.965 1.00 63.52 C ATOM 667 CB ASP A 131 18.635 13.541 −9.106 1.00 57.78 C ATOM 668 CG ASP A 131 19.204 13.644 −10.483 1.00 58.59 C ATOM 669 OD1 ASP A 131 18.960 12.714 −11.274 1.00 56.65 O ATOM 670 OD2 ASP A 131 19.901 14.638 −10.776 1.00 63.56 O ATOM 671 C ASP A 131 17.369 12.131 −7.495 1.00 56.89 C ATOM 672 O ASP A 131 18.045 11.341 −6.841 1.00 65.85 O ATOM 673 N LEU A 132 16.357 12.819 −6.976 1.00 54.41 N ATOM 674 CA LEU A 132 16.058 12.756 −5.550 1.00 58.87 C ATOM 675 CB LEU A 132 16.554 14.020 −4.836 1.00 57.96 C ATOM 676 CG LEU A 132 18.055 14.218 −4.597 1.00 60.62 C ATOM 677 CD1 LEU A 132 18.344 15.614 −4.041 1.00 58.05 C ATOM 678 CD2 LEU A 132 18.596 13.156 −3.666 1.00 56.51 C ATOM 679 C LEU A 132 14.573 12.561 −5.291 1.00 60.00 C ATOM 680 O LEU A 132 13.741 12.949 −6.117 1.00 61.71 O ATOM 681 N PRO A 133 14.238 11.962 −4.132 1.00 57.32 N ATOM 682 CD PRO A 133 15.202 11.583 −3.079 1.00 58.89 C ATOM 683 CA PRO A 133 12.846 11.726 −3.733 1.00 50.66 C ATOM 684 CB PRO A 133 12.960 11.323 −2.266 1.00 53.17 C ATOM 685 CG PRO A 133 14.363 10.818 −2.100 1.00 58.39 C ATOM 686 C PRO A 133 12.061 13.021 −3.842 1.00 58.70 C ATOM 687 O PRO A 133 12.621 14.083 −3.595 1.00 56.85 O ATOM 688 N ARG A 134 10.786 12.934 −4.202 1.00 59.56 N ATOM 689 CA ARG A 134 9.987 14.128 −4.415 1.00 54.62 C ATOM 690 CB ARG A 134 8.615 13.771 −4.975 1.00 56.38 C ATOM 691 CG ARG A 134 8.556 13.834 −6.485 1.00 62.19 C ATOM 692 CD ARG A 134 7.170 13.544 −7.025 1.00 60.70 C ATOM 693 NE ARG A 134 7.137 13.801 −8.459 1.00 63.59 N ATOM 694 CZ ARG A 134 6.123 13.495 −9.261 1.00 69.57 C ATOM 695 NH1 ARG A 134 5.035 12.901 −8.776 1.00 69.93 N ATOM 696 NH2 ARG A 134 6.204 13.781 −10.555 1.00 64.83 N ATOM 697 C ARG A 134 9.842 14.982 −3.167 1.00 58.11 C ATOM 698 O ARG A 134 9.566 16.178 −3.261 1.00 63.16 O ATOM 699 N ALA A 135 10.024 14.381 −2.000 1.00 56.02 N ATOM 700 CA ALA A 135 9.810 15.109 −0.759 1.00 52.35 C ATOM 701 CB ALA A 135 9.305 14.186 0.327 1.00 43.52 C ATOM 702 C ALA A 135 11.099 15.775 −0.325 1.00 55.56 C ATOM 703 O ALA A 135 11.077 16.863 0.245 1.00 54.92 O ATOM 704 N VAL A 136 12.223 15.117 −0.593 1.00 52.58 N ATOM 705 CA VAL A 136 13.517 15.667 −0.232 1.00 50.72 C ATOM 706 CB VAL A 136 14.635 14.651 −0.451 1.00 52.90 C ATOM 707 CG1 VAL A 136 16.001 15.310 −0.270 1.00 42.40 C ATOM 708 CG2 VAL A 136 14.457 13.494 0.527 1.00 52.44 C ATOM 709 C VAL A 136 13.776 16.938 −1.021 1.00 50.44 C ATOM 710 O VAL A 136 14.432 17.863 −0.550 1.00 51.17 O ATOM 711 N ILE A 137 13.227 16.992 −2.224 1.00 53.51 N ATOM 712 CA ILE A 137 13.340 18.187 −3.039 1.00 52.94 C ATOM 713 CB ILE A 137 13.025 17.888 −4.516 1.00 51.55 C ATOM 714 CG2 ILE A 137 12.849 19.176 −5.292 1.00 45.79 C ATOM 715 CG1 ILE A 137 14.147 17.037 −5.113 1.00 52.71 C ATOM 716 CD1 ILE A 137 13.687 16.080 −6.214 1.00 54.01 C ATOM 717 C ILE A 137 12.429 19.286 −2.496 1.00 51.67 C ATOM 718 O ILE A 137 12.824 20.454 −2.451 1.00 48.38 O ATOM 719 N ASP A 138 11.216 18.911 −2.087 1.00 48.65 N ATOM 720 CA ASP A 138 10.272 19.868 −1.517 1.00 46.45 C ATOM 721 CB ASP A 138 8.965 19.184 −1.096 1.00 55.18 C ATOM 722 CG ASP A 138 8.173 18.642 −2.277 1.00 55.74 C ATOM 723 OD1 ASP A 138 8.740 18.525 −3.381 1.00 56.81 O ATOM 724 OD2 ASP A 138 6.984 18.320 −2.090 1.00 55.45 O ATOM 725 C ASP A 138 10.886 20.523 −0.303 1.00 47.83 C ATOM 726 O ASP A 138 10.815 21.735 −0.140 1.00 48.09 O ATOM 727 N ASP A 139 11.475 19.693 0.555 1.00 47.28 N ATOM 728 CA ASP A 139 12.128 20.146 1.769 1.00 41.04 C ATOM 729 CB ASP A 139 12.678 18.932 2.530 1.00 44.11 C ATOM 730 CG ASP A 139 13.262 19.292 3.899 1.00 48.61 C ATOM 731 OD1 ASP A 139 12.597 20.034 4.658 1.00 51.68 O ATOM 732 OD2 ASP A 139 14.374 18.811 4.231 1.00 44.98 O ATOM 733 C ASP A 139 13.267 21.093 1.390 1.00 52.33 C ATOM 734 O ASP A 139 13.434 22.167 1.981 1.00 52.55 O ATOM 735 N ALA A 140 14.052 20.702 0.393 1.00 43.10 N ATOM 736 CA ALA A 140 15.226 21.478 0.050 1.00 47.68 C ATOM 737 CB ALA A 140 15.971 20.821 −1.077 1.00 51.10 C ATOM 738 C ALA A 140 14.902 22.946 −0.283 1.00 52.75 C ATOM 739 O ALA A 140 15.555 23.861 0.218 1.00 52.15 O ATOM 740 N PHE A 141 13.899 23.184 −1.120 1.00 50.14 N ATOM 741 CA PHE A 141 13.520 24.566 −1.404 1.00 53.45 C ATOM 742 CB PHE A 141 12.498 24.650 −2.531 1.00 54.87 C ATOM 743 CG PHE A 141 12.913 23.950 −3.781 1.00 48.87 C ATOM 744 CD1 PHE A 141 14.196 24.058 −4.252 1.00 51.65 C ATOM 745 CD2 PHE A 141 12.003 23.192 −4.494 1.00 49.59 C ATOM 746 CE1 PHE A 141 14.568 23.415 −5.417 1.00 53.48 C ATOM 747 CE2 PHE A 141 12.364 22.549 −5.649 1.00 50.79 C ATOM 748 CZ PHE A 141 13.648 22.661 −6.115 1.00 49.43 C ATOM 749 C PHE A 141 12.926 25.192 −0.153 1.00 50.30 C ATOM 750 O PHE A 141 13.056 26.392 0.096 1.00 52.28 O ATOM 751 N ALA A 142 12.261 24.377 0.642 1.00 48.19 N ATOM 752 CA ALA A 142 11.694 24.894 1.871 1.00 53.15 C ATOM 753 CB ALA A 142 10.948 23.796 2.616 1.00 52.48 C ATOM 754 C ALA A 142 12.791 25.523 2.746 1.00 50.60 C ATOM 755 O ALA A 142 12.665 26.676 3.151 1.00 50.34 O ATOM 756 N ARG A 143 13.863 24.774 3.021 1.00 49.08 N ATOM 757 CA ARG A 143 14.978 25.284 3.835 1.00 42.49 C ATOM 758 CB ARG A 143 15.932 24.161 4.193 1.00 34.70 C ATOM 759 CG ARG A 143 15.318 23.148 5.122 1.00 41.26 C ATOM 760 CD ARG A 143 15.649 21.724 4.719 1.00 46.44 C ATOM 761 NE ARG A 143 17.023 21.376 5.042 1.00 46.63 N ATOM 762 CZ ARG A 143 17.998 21.284 4.144 1.00 45.17 C ATOM 763 NH1 ARG A 143 17.746 21.480 2.861 1.00 49.07 N ATOM 764 NH2 ARG A 143 19.220 20.973 4.529 1.00 43.86 N ATOM 765 C ARG A 143 15.730 26.401 3.110 1.00 48.00 C ATOM 766 O ARG A 143 16.179 27.366 3.736 1.00 45.35 O ATOM 767 N ALA A 144 15.859 26.267 1.788 1.00 46.04 N ATOM 768 CA ALA A 144 16.364 27.345 0.953 1.00 44.10 C ATOM 769 CB ALA A 144 16.292 26.966 −0.518 1.00 46.85 C ATOM 770 C ALA A 144 15.540 28.603 1.212 1.00 49.14 C ATOM 771 O ALA A 144 16.090 29.694 1.361 1.00 47.79 O ATOM 772 N PHE A 145 14.219 28.448 1.287 1.00 47.35 N ATOM 773 CA PHE A 145 13.342 29.588 1.564 1.00 46.16 C ATOM 774 CB PHE A 145 11.908 29.284 1.154 1.00 41.62 C ATOM 775 CG PHE A 145 11.686 29.430 −0.318 1.00 48.58 C ATOM 776 CD1 PHE A 145 12.144 30.555 −0.974 1.00 43.41 C ATOM 777 CD2 PHE A 145 11.048 28.445 −1.048 1.00 48.39 C ATOM 778 CE1 PHE A 145 11.957 30.709 −2.325 1.00 46.76 C ATOM 779 CE2 PHE A 145 10.864 28.581 −2.402 1.00 46.25 C ATOM 780 CZ PHE A 145 11.320 29.717 −3.048 1.00 50.47 C ATOM 781 C PHE A 145 13.420 30.113 2.998 1.00 40.67 C ATOM 782 O PHE A 145 13.259 31.310 3.241 1.00 38.32 O ATOM 783 N ALA A 146 13.708 29.226 3.937 1.00 40.24 N ATOM 784 CA ALA A 146 13.761 29.628 5.337 1.00 42.13 C ATOM 785 CB ALA A 146 13.827 28.422 6.218 1.00 40.37 C ATOM 786 C ALA A 146 14.942 30.558 5.599 1.00 40.98 C ATOM 787 O ALA A 146 14.968 31.286 6.590 1.00 40.58 O ATOM 788 N LEU A 147 15.914 30.530 4.695 1.00 43.94 N ATOM 789 CA LEU A 147 17.032 31.465 4.736 1.00 40.50 C ATOM 790 CB LEU A 147 18.075 31.034 3.719 1.00 40.68 C ATOM 791 CG LEU A 147 18.563 29.622 4.016 1.00 46.09 C ATOM 792 CD1 LEU A 147 19.561 29.146 2.962 1.00 41.15 C ATOM 793 CD2 LEU A 147 19.175 29.560 5.444 1.00 41.82 C ATOM 794 C LEU A 147 16.624 32.933 4.498 1.00 43.00 C ATOM 795 O LEU A 147 17.091 33.838 5.188 1.00 41.55 O ATOM 796 N TRP A 148 15.775 33.195 3.536 1.00 40.29 N ATOM 797 CA TRP A 148 15.367 34.532 3.259 1.00 35.66 C ATOM 798 CB TRP A 148 15.089 34.675 1.785 1.00 46.95 C ATOM 799 CG TRP A 148 16.165 34.135 0.929 1.00 43.32 C ATOM 800 CD2 TRP A 148 17.402 34.757 0.630 1.00 39.54 C ATOM 801 CE2 TRP A 148 18.109 33.892 −0.181 1.00 37.83 C ATOM 802 CE3 TRP A 148 17.987 35.962 0.994 1.00 44.81 C ATOM 803 CD1 TRP A 148 16.172 32.964 0.295 1.00 39.40 C ATOM 804 NE1 TRP A 148 17.328 32.801 −0.381 1.00 41.00 N ATOM 805 CZ2 TRP A 148 19.338 34.188 −0.658 1.00 40.65 C ATOM 806 CZ3 TRP A 148 19.203 36.244 0.529 1.00 46.86 C ATOM 807 CH2 TRP A 148 19.874 35.368 −0.297 1.00 43.87 C ATOM 808 C TRP A 148 14.167 34.901 4.060 1.00 42.66 C ATOM 809 O TRP A 148 13.978 36.017 4.386 1.00 46.11 O ATOM 810 N SER A 149 13.346 33.948 4.401 1.00 42.98 N ATOM 811 CA SER A 149 12.210 34.201 5.260 1.00 41.79 C ATOM 812 CB SER A 149 11.547 32.891 5.575 1.00 40.04 C ATOM 813 OG SER A 149 10.170 33.005 5.609 1.00 50.50 O ATOM 814 C SER A 149 12.555 34.872 6.565 1.00 42.14 C ATOM 815 O SER A 149 11.781 35.610 7.097 1.00 45.42 O ATOM 816 N ALA A 150 13.714 34.587 7.096 1.00 42.48 N ATOM 817 CA ALA A 150 14.053 34.954 8.443 1.00 46.15 C ATOM 818 CB ALA A 150 14.933 33.940 8.999 1.00 41.25 C ATOM 819 C ALA A 150 14.716 36.305 8.507 1.00 47.05 C ATOM 820 O ALA A 150 14.711 36.983 9.500 1.00 49.66 O ATOM 821 N VAL A 151 15.279 36.705 7.405 1.00 45.53 N ATOM 822 CA VAL A 151 15.974 37.994 7.336 1.00 50.74 C ATOM 823 CB VAL A 151 17.377 37.835 6.745 1.00 41.06 C ATOM 824 CG1 VAL A 151 18.277 37.086 7.723 1.00 39.90 C ATOM 825 CG2 VAL A 151 17.286 37.100 5.442 1.00 39.94 C ATOM 826 C VAL A 151 15.198 38.984 6.484 1.00 48.07 C ATOM 827 O VAL A 151 15.746 39.963 5.980 1.00 43.98 O ATOM 828 N THR A 152 13.905 38.733 6.352 1.00 48.63 N ATOM 829 CA THR A 152 13.091 39.489 5.432 1.00 44.47 C ATOM 830 CB THR A 152 12.989 38.740 4.103 1.00 45.61 C ATOM 831 OG1 THR A 152 14.257 38.772 3.433 1.00 56.33 O ATOM 832 CG2 THR A 152 12.021 39.407 3.245 1.00 50.13 C ATOM 833 C THR A 152 11.689 39.638 5.972 1.00 50.10 C ATOM 834 O THR A 152 11.172 38.734 6.641 1.00 53.26 O ATOM 835 N PRO A 153 11.048 40.773 5.676 1.00 54.38 N ATOM 836 CD PRO A 153 11.596 42.013 5.102 1.00 52.17 C ATOM 837 CA PRO A 153 9.617 40.876 5.986 1.00 56.42 C ATOM 838 CB PRO A 153 9.277 42.322 5.602 1.00 56.68 C ATOM 839 CG PRO A 153 10.605 43.037 5.511 1.00 57.40 C ATOM 840 C PRO A 153 8.774 39.915 5.136 1.00 48.71 C ATOM 841 O PRO A 153 7.585 40.155 4.998 1.00 52.07 O ATOM 842 N LEU A 154 9.371 38.856 4.592 1.00 45.44 N ATOM 843 CA LEU A 154 8.689 37.990 3.636 1.00 42.28 C ATOM 844 CB LEU A 154 9.524 37.836 2.367 1.00 47.45 C ATOM 845 CG LEU A 154 9.814 39.088 1.528 1.00 45.20 C ATOM 846 CD1 LEU A 154 10.676 38.713 0.349 1.00 48.79 C ATOM 847 CD2 LEU A 154 8.539 39.788 1.079 1.00 49.22 C ATOM 848 C LEU A 154 8.392 36.613 4.199 1.00 46.05 C ATOM 849 O LEU A 154 9.013 36.188 5.175 1.00 49.29 O ATOM 850 N THR A 155 7.446 35.919 3.567 1.00 46.78 N ATOM 851 CA THR A 155 7.081 34.545 3.913 1.00 43.49 C ATOM 852 CB THR A 155 5.749 34.491 4.664 1.00 47.19 C ATOM 853 OG1 THR A 155 4.734 35.083 3.842 1.00 49.71 O ATOM 854 CG2 THR A 155 5.826 35.230 6.015 1.00 33.55 C ATOM 855 C THR A 155 6.885 33.797 2.603 1.00 44.20 C ATOM 856 O THR A 155 6.467 34.394 1.616 1.00 51.76 O ATOM 857 N PHE A 156 7.162 32.500 2.583 1.00 39.99 N ATOM 858 CA PHE A 156 7.125 31.740 1.330 1.00 46.29 C ATOM 859 CB PHE A 156 8.523 31.287 0.894 1.00 38.38 C ATOM 860 CG PHE A 156 9.489 32.412 0.740 1.00 41.91 C ATOM 861 CD1 PHE A 156 10.369 32.729 1.759 1.00 40.06 C ATOM 862 CD2 PHE A 156 9.493 33.175 −0.409 1.00 40.58 C ATOM 863 CE1 PHE A 156 11.240 33.776 1.629 1.00 42.24 C ATOM 864 CE2 PHE A 156 10.372 34.228 −0.557 1.00 45.33 C ATOM 865 CZ PHE A 156 11.250 34.530 0.465 1.00 46.60 C ATOM 866 C PHE A 156 6.251 30.532 1.509 1.00 53.18 C ATOM 867 O PHE A 156 6.548 29.650 2.318 1.00 57.07 O ATOM 868 N THR A 157 5.165 30.489 0.758 1.00 47.16 N ATOM 869 CA THR A 157 4.156 29.479 0.998 1.00 50.89 C ATOM 870 CB THR A 157 2.885 30.109 1.563 1.00 51.48 C ATOM 871 OG1 THR A 157 2.140 30.730 0.511 1.00 53.11 O ATOM 872 CG2 THR A 157 3.246 31.162 2.566 1.00 47.51 C ATOM 873 C THR A 157 3.862 28.781 −0.312 1.00 61.69 C ATOM 874 O THR A 157 3.648 29.428 −1.341 1.00 61.07 O ATOM 875 N ARG A 158 3.884 27.457 −0.270 1.00 60.04 N ATOM 876 CA ARG A 158 3.744 26.656 −1.469 1.00 54.30 C ATOM 877 CB ARG A 158 4.073 25.202 −1.169 1.00 54.29 C ATOM 878 CG ARG A 158 4.130 24.345 −2.397 1.00 59.50 C ATOM 879 CD ARG A 158 4.631 22.975 −2.036 1.00 62.36 C ATOM 880 NE ARG A 158 5.045 22.226 −3.212 1.00 68.40 N ATOM 881 CZ ARG A 158 5.204 20.907 −3.227 1.00 70.93 C ATOM 882 NH1 ARG A 158 4.967 20.200 −2.121 1.00 59.90 N ATOM 883 NH2 ARG A 158 5.589 20.300 −4.350 1.00 62.22 N ATOM 884 C ARG A 158 2.349 26.767 −2.064 1.00 60.56 C ATOM 885 O ARG A 158 1.359 26.931 −1.350 1.00 60.65 O ATOM 886 N VAL A 159 2.290 26.694 −3.388 1.00 62.86 N ATOM 887 CA VAL A 159 1.033 26.775 −4.122 1.00 63.91 C ATOM 888 CB VAL A 159 0.758 28.237 −4.619 1.00 62.39 C ATOM 889 CG1 VAL A 159 −0.184 28.276 −5.818 1.00 61.38 C ATOM 890 CG2 VAL A 159 0.211 29.098 −3.474 1.00 65.00 C ATOM 891 C VAL A 159 1.119 25.771 −5.271 1.00 60.80 C ATOM 892 O VAL A 159 2.189 25.234 −5.558 1.00 58.76 O ATOM 893 N TYR A 160 −0.006 25.494 −5.910 1.00 62.31 N ATOM 894 CA TYR A 160 −0.004 24.563 −7.022 1.00 62.15 C ATOM 895 CB TYR A 160 −0.613 23.239 −6.585 1.00 63.25 C ATOM 896 CG TYR A 160 0.103 22.654 −5.393 1.00 65.40 C ATOM 897 CD1 TYR A 160 −0.421 22.771 −4.115 1.00 62.84 C ATOM 898 CE1 TYR A 160 0.247 22.231 −3.015 1.00 68.16 C ATOM 899 CD2 TYR A 160 1.318 22.002 −5.547 1.00 63.13 C ATOM 900 CE2 TYR A 160 1.986 21.458 −4.467 1.00 66.36 C ATOM 901 CZ TYR A 160 1.454 21.575 −3.201 1.00 71.07 C ATOM 902 OH TYR A 160 2.133 21.031 −2.127 1.00 67.08 O ATOM 903 C TYR A 160 −0.713 25.133 −8.240 1.00 58.69 C ATOM 904 O TYR A 160 −1.575 24.490 −8.822 1.00 65.06 O ATOM 905 N SER A 161 −0.342 26.350 −8.615 1.00 59.67 N ATOM 906 CA SER A 161 −0.844 26.962 −9.836 1.00 61.50 C ATOM 907 CB SER A 161 −1.983 27.916 −9.521 1.00 68.69 C ATOM 908 OG SER A 161 −1.477 29.100 −8.931 1.00 70.11 O ATOM 909 C SER A 161 0.267 27.758 −10.486 1.00 62.83 C ATOM 910 O SER A 161 1.244 28.117 −9.835 1.00 67.08 O ATOM 911 N ARG A 162 0.106 28.048 −11.767 1.00 65.92 N ATOM 912 CA ARG A 162 1.047 28.885 −12.497 1.00 66.39 C ATOM 913 CB ARG A 162 0.758 28.795 −14.004 1.00 68.03 C ATOM 914 CG ARG A 162 1.509 29.799 −14.845 1.00 65.55 C ATOM 915 CD ARG A 162 0.672 30.276 −16.024 1.00 69.12 C ATOM 916 NE ARG A 162 1.114 31.596 −16.473 1.00 71.45 N ATOM 917 CZ ARG A 162 0.317 32.654 −16.593 1.00 68.81 C ATOM 918 NH1 ARG A 162 −0.976 32.543 −16.316 1.00 61.94 N ATOM 919 NH2 ARG A 162 0.814 33.820 −16.999 1.00 67.09 N ATOM 920 C ARG A 162 0.944 30.333 −12.013 1.00 60.96 C ATOM 921 O ARG A 162 1.595 31.234 −12.538 1.00 66.32 O ATOM 922 N ASP A 163 0.116 30.554 −11.000 1.00 62.31 N ATOM 923 CA ASP A 163 −0.090 31.903 −10.487 1.00 64.42 C ATOM 924 CB ASP A 163 −1.554 32.094 −10.055 1.00 68.30 C ATOM 925 CG ASP A 163 −2.500 32.344 −11.246 1.00 78.68 C ATOM 926 OD1 ASP A 163 −3.737 32.356 −11.036 1.00 79.69 O ATOM 927 OD2 ASP A 163 −2.007 32.536 −12.389 1.00 71.29 O ATOM 928 C ASP A 163 0.890 32.261 −9.354 1.00 63.28 C ATOM 929 O ASP A 163 0.757 33.294 −8.698 1.00 59.58 O ATOM 930 N ALA A 164 1.886 31.412 −9.138 1.00 54.14 N ATOM 931 CA ALA A 164 2.888 31.700 −8.134 1.00 51.79 C ATOM 932 CB ALA A 164 3.650 30.438 −7.776 1.00 50.49 C ATOM 933 C ALA A 164 3.838 32.808 −8.604 1.00 55.68 C ATOM 934 O ALA A 164 4.110 32.944 −9.801 1.00 49.33 O ATOM 935 N ASP A 165 4.319 33.610 −7.655 1.00 55.23 N ATOM 936 CA ASP A 165 5.347 34.615 −7.933 1.00 55.28 C ATOM 937 CB ASP A 165 5.639 35.452 −6.687 1.00 51.88 C ATOM 938 CG ASP A 165 4.381 35.971 −6.020 1.00 50.57 C ATOM 939 OD1 ASP A 165 4.337 35.977 −4.777 1.00 51.31 O ATOM 940 OD2 ASP A 165 3.432 36.361 −6.727 1.00 52.39 O ATOM 941 C ASP A 165 6.632 33.934 −8.399 1.00 55.38 C ATOM 942 O ASP A 165 7.375 34.462 −9.239 1.00 51.18 O ATOM 943 N ILE A 166 6.885 32.752 −7.849 1.00 51.66 N ATOM 944 CA ILE A 166 8.071 31.989 −8.201 1.00 50.35 C ATOM 945 CB ILE A 166 9.007 31.837 −6.988 1.00 48.22 C ATOM 946 CG2 ILE A 166 10.308 31.145 −7.393 1.00 41.37 C ATOM 947 CG1 ILE A 166 9.264 33.203 −6.346 1.00 50.60 C ATOM 948 CD1 ILE A 166 9.997 33.131 −5.032 1.00 47.43 C ATOM 949 C ILE A 166 7.730 30.600 −8.709 1.00 46.18 C ATOM 950 O ILE A 166 7.395 29.718 −7.929 1.00 49.23 O ATOM 951 N VAL A 167 7.831 30.398 −10.015 1.00 49.37 N ATOM 952 CA VAL A 167 7.687 29.057 −10.583 1.00 48.82 C ATOM 953 CB VAL A 167 7.080 29.106 −11.989 1.00 47.51 C ATOM 954 CG1 VAL A 167 7.039 27.711 −12.586 1.00 44.72 C ATOM 955 CG2 VAL A 167 5.685 29.721 −11.922 1.00 52.98 C ATOM 956 C VAL A 167 9.036 28.332 −10.623 1.00 45.84 C ATOM 957 O VAL A 167 10.023 28.886 −11.089 1.00 48.16 O ATOM 958 N ILE A 168 9.068 27.096 −10.136 1.00 44.26 N ATOM 959 CA ILE A 168 10.304 26.333 −10.007 1.00 44.87 C ATOM 960 CB ILE A 168 10.465 25.760 −8.577 1.00 35.26 C ATOM 961 CG2 ILE A 168 11.492 24.665 −8.534 1.00 36.99 C ATOM 962 CG1 ILE A 168 10.842 26.881 −7.608 1.00 46.12 C ATOM 963 CD1 ILE A 168 11.068 26.411 −6.160 1.00 49.98 C ATOM 964 C ILE A 168 10.296 25.196 −11.015 1.00 50.66 C ATOM 965 O ILE A 168 9.410 24.341 −10.986 1.00 50.30 O ATOM 966 N GLN A 169 11.291 25.173 −11.897 1.00 50.08 N ATOM 967 CA GLN A 169 11.284 24.211 −12.995 1.00 53.72 C ATOM 968 CB GLN A 169 10.750 24.882 −14.265 1.00 46.79 C ATOM 969 CG GLN A 169 10.689 23.991 −15.480 1.00 64.45 C ATOM 970 CD GLN A 169 10.465 24.772 −16.777 1.00 59.89 C ATOM 971 OE1 GLN A 169 10.985 24.401 −17.845 1.00 49.02 O ATOM 972 NE2 GLN A 169 9.703 25.867 −16.682 1.00 49.76 N ATOM 973 C GLN A 169 12.652 23.570 −13.233 1.00 56.08 C ATOM 974 O GLN A 169 13.702 24.217 −13.117 1.00 55.18 O ATOM 975 N PHE A 170 12.641 22.282 −13.548 1.00 59.25 N ATOM 976 CA PHE A 170 13.869 21.614 −13.962 1.00 62.40 C ATOM 977 CB PHE A 170 13.971 20.214 −13.346 1.00 61.44 C ATOM 978 CG PHE A 170 14.337 20.221 −11.883 1.00 54.84 C ATOM 979 CD1 PHE A 170 13.368 20.400 −10.911 1.00 61.39 C ATOM 980 CD2 PHE A 170 15.649 20.053 −11.484 1.00 55.53 C ATOM 981 CE1 PHE A 170 13.703 20.404 −9.557 1.00 58.71 C ATOM 982 CE2 PHE A 170 15.993 20.059 −10.138 1.00 56.87 C ATOM 983 CZ PHE A 170 15.015 20.234 −9.174 1.00 51.70 C ATOM 984 C PHE A 170 13.924 21.569 −15.485 1.00 55.03 C ATOM 985 O PHE A 170 12.983 21.109 −16.119 1.00 64.02 O ATOM 986 N GLY A 171 15.020 22.071 −16.049 1.00 54.40 N ATOM 987 CA GLY A 171 15.187 22.244 −17.484 1.00 55.97 C ATOM 988 C GLY A 171 16.429 21.561 −18.042 1.00 60.39 C ATOM 989 O GLY A 171 17.487 21.515 −17.402 1.00 53.11 O ATOM 990 N VAL A 172 16.298 21.041 −19.257 1.00 58.51 N ATOM 991 CA VAL A 172 17.267 20.098 −19.785 1.00 59.94 C ATOM 992 CB VAL A 172 16.546 18.809 −20.296 1.00 61.75 C ATOM 993 CG1 VAL A 172 15.878 19.052 −21.640 1.00 65.46 C ATOM 994 CG2 VAL A 172 17.494 17.614 −20.351 1.00 58.11 C ATOM 995 C VAL A 172 18.202 20.734 −20.838 1.00 65.80 C ATOM 996 O VAL A 172 19.381 20.358 −20.936 1.00 66.45 O ATOM 997 N ALA A 173 17.698 21.708 −21.598 1.00 56.07 N ATOM 998 CA ALA A 173 18.553 22.465 −22.520 1.00 58.21 C ATOM 999 CB ALA A 173 18.967 21.603 −23.695 1.00 63.37 C ATOM 1000 C ALA A 173 17.858 23.742 −23.000 1.00 58.73 C ATOM 1001 O ALA A 173 17.923 24.769 −22.338 1.00 58.63 O ATOM 1002 N GLU A 174 17.209 23.694 −24.156 1.00 56.78 N ATOM 1003 CA GLU A 174 16.247 24.739 −24.484 1.00 58.60 C ATOM 1004 CB GLU A 174 15.962 24.808 −25.989 1.00 58.47 C ATOM 1005 CG GLU A 174 17.176 25.064 −26.864 1.00 57.98 C ATOM 1006 CD GLU A 174 17.883 23.774 −27.249 1.00 61.53 C ATOM 1007 OE1 GLU A 174 19.101 23.818 −27.554 1.00 53.03 O ATOM 1008 OE2 GLU A 174 17.210 22.715 −27.247 1.00 61.26 O ATOM 1009 C GLU A 174 14.980 24.374 −23.728 1.00 59.08 C ATOM 1010 O GLU A 174 14.461 23.267 −23.899 1.00 60.24 O ATOM 1011 N HIS A 175 14.485 25.279 −22.885 1.00 56.10 N ATOM 1012 CA HIS A 175 13.386 24.912 −21.984 1.00 54.26 C ATOM 1013 CB HIS A 175 13.923 24.495 −20.603 1.00 56.94 C ATOM 1014 CG HIS A 175 14.908 25.455 −20.011 1.00 56.06 C ATOM 1015 CD2 HIS A 175 14.922 26.102 −18.820 1.00 57.78 C ATOM 1016 ND1 HIS A 175 16.074 25.814 −20.653 1.00 56.52 N ATOM 1017 CE1 HIS A 175 16.760 26.645 −19.887 1.00 53.82 C ATOM 1018 NE2 HIS A 175 16.084 26.834 −18.769 1.00 52.52 N ATOM 1019 C HIS A 175 12.273 25.945 −21.833 1.00 53.30 C ATOM 1020 O HIS A 175 11.758 26.165 −20.737 1.00 52.33 O ATOM 1021 N GLY A 176 11.886 26.565 −22.940 1.00 59.44 N ATOM 1022 CA GLY A 176 10.732 27.439 −22.933 1.00 57.49 C ATOM 1023 C GLY A 176 11.028 28.874 −22.563 1.00 57.21 C ATOM 1024 O GLY A 176 10.099 29.659 −22.348 1.00 46.99 O ATOM 1025 N ASP A 177 12.318 29.202 −22.463 1.00 55.71 N ATOM 1026 CA ASP A 177 12.781 30.594 −22.355 1.00 49.16 C ATOM 1027 CB ASP A 177 12.958 31.049 −20.901 1.00 53.35 C ATOM 1028 CG ASP A 177 14.239 30.511 −20.254 1.00 59.24 C ATOM 1029 OD1 ASP A 177 15.041 29.832 −20.952 1.00 56.28 O ATOM 1030 OD2 ASP A 177 14.443 30.785 −19.037 1.00 55.75 O ATOM 1031 C ASP A 177 14.078 30.760 −23.137 1.00 54.31 C ATOM 1032 O ASP A 177 14.553 29.804 −23.776 1.00 49.71 O ATOM 1033 N GLY A 178 14.651 31.963 −23.069 1.00 53.23 N ATOM 1034 CA GLY A 178 15.790 32.332 −23.901 1.00 53.76 C ATOM 1035 C GLY A 178 17.185 31.993 −23.391 1.00 51.89 C ATOM 1036 O GLY A 178 18.190 32.474 −23.923 1.00 51.16 O ATOM 1037 N TYR A 179 17.254 31.149 −22.369 1.00 54.02 N ATOM 1038 CA TYR A 179 18.527 30.874 −21.715 1.00 54.93 C ATOM 1039 CB TYR A 179 18.624 31.689 −20.427 1.00 50.33 C ATOM 1040 CG TYR A 179 18.518 33.183 −20.654 1.00 48.16 C ATOM 1041 CD1 TYR A 179 17.292 33.834 −20.634 1.00 44.22 C ATOM 1042 CE1 TYR A 179 17.208 35.217 −20.836 1.00 46.44 C ATOM 1043 CD2 TYR A 179 19.657 33.940 −20.901 1.00 51.78 C ATOM 1044 CE2 TYR A 179 19.589 35.315 −21.106 1.00 48.83 C ATOM 1045 CZ TYR A 179 18.369 35.953 −21.072 1.00 49.80 C ATOM 1046 OH TYR A 179 18.344 37.323 −21.285 1.00 46.18 O ATOM 1047 C TYR A 179 18.686 29.373 −21.452 1.00 57.76 C ATOM 1048 O TYR A 179 18.311 28.867 −20.385 1.00 49.73 O ATOM 1049 N PRO A 180 19.255 28.662 −22.436 1.00 52.97 N ATOM 1050 CD PRO A 180 20.033 29.239 −23.544 1.00 46.49 C ATOM 1051 CA PRO A 180 19.266 27.202 −22.465 1.00 47.45 C ATOM 1052 CB PRO A 180 19.731 26.886 −23.896 1.00 53.37 C ATOM 1053 CG PRO A 180 19.863 28.224 −24.606 1.00 47.28 C ATOM 1054 C PRO A 180 20.314 26.714 −21.509 1.00 46.35 C ATOM 1055 O PRO A 180 21.287 27.442 −21.343 1.00 49.14 O ATOM 1056 N PHE A 181 20.136 25.540 −20.900 1.00 46.81 N ATOM 1057 CA PHE A 181 21.193 24.946 −20.082 1.00 47.61 C ATOM 1058 CB PHE A 181 20.636 24.069 −18.954 1.00 47.78 C ATOM 1059 CG PHE A 181 19.750 24.816 −17.997 1.00 48.71 C ATOM 1060 CD1 PHE A 181 20.162 26.015 −17.453 1.00 47.19 C ATOM 1061 CD2 PHE A 181 18.503 24.324 −17.655 1.00 55.33 C ATOM 1062 CE1 PHE A 181 19.347 26.711 −16.590 1.00 52.30 C ATOM 1063 CE2 PHE A 181 17.677 25.016 −16.790 1.00 55.32 C ATOM 1064 CZ PHE A 181 18.099 26.213 −16.258 1.00 54.58 C ATOM 1065 C PHE A 181 22.165 24.179 −20.974 1.00 51.29 C ATOM 1066 O PHE A 181 21.806 23.716 −22.057 1.00 46.73 O ATOM 1067 N ASP A 182 23.400 24.054 −20.510 1.00 51.87 N ATOM 1068 CA ASP A 182 24.493 23.716 −21.404 1.00 52.12 C ATOM 1069 CB ASP A 182 25.698 24.611 −21.095 1.00 45.01 C ATOM 1070 CG ASP A 182 26.265 24.369 −19.709 1.00 54.41 C ATOM 1071 OD1 ASP A 182 25.716 23.521 −18.966 1.00 51.77 O ATOM 1072 OD2 ASP A 182 27.271 25.025 −19.372 1.00 49.48 O ATOM 1073 C ASP A 182 24.890 22.238 −21.402 1.00 52.35 C ATOM 1074 O ASP A 182 25.909 21.869 −21.980 1.00 54.14 O ATOM 1075 N GLY A 183 24.082 21.389 −20.782 1.00 48.83 N ATOM 1076 CA GLY A 183 24.471 20.007 −20.612 1.00 47.30 C ATOM 1077 C GLY A 183 25.030 19.784 −19.218 1.00 56.45 C ATOM 1078 O GLY A 183 24.578 20.389 −18.248 1.00 58.00 O ATOM 1079 N LYS A 184 26.019 18.913 −19.102 1.00 48.37 N ATOM 1080 CA LYS A 184 26.504 18.527 −17.779 1.00 59.51 C ATOM 1081 CB LYS A 184 26.891 17.044 −17.775 1.00 57.49 C ATOM 1082 CG LYS A 184 27.575 16.579 −16.506 1.00 58.19 C ATOM 1083 CD LYS A 184 28.083 15.157 −16.684 1.00 63.70 C ATOM 1084 CE LYS A 184 29.148 14.783 −15.648 1.00 65.63 C ATOM 1085 NZ LYS A 184 28.581 14.438 −14.298 1.00 63.05 N ATOM 1086 C LYS A 184 27.670 19.386 −17.272 1.00 57.03 C ATOM 1087 O LYS A 184 28.541 19.780 −18.037 1.00 63.33 O ATOM 1088 N ASP A 185 27.669 19.675 −15.978 1.00 59.84 N ATOM 1089 CA ASP A 185 28.799 20.343 −15.317 1.00 63.87 C ATOM 1090 CB ASP A 185 30.119 19.620 −15.622 1.00 61.03 C ATOM 1091 CG ASP A 185 30.367 18.439 −14.707 1.00 63.09 C ATOM 1092 OD1 ASP A 185 30.080 18.556 −13.492 1.00 64.82 O ATOM 1093 OD2 ASP A 185 30.860 17.396 −15.206 1.00 57.74 O ATOM 1094 C ASP A 185 28.987 21.837 −15.598 1.00 59.82 C ATOM 1095 O ASP A 185 29.849 22.466 −14.986 1.00 63.67 O ATOM 1096 N GLY A 186 28.217 22.408 −16.515 1.00 52.41 N ATOM 1097 CA GLY A 186 28.471 23.783 −16.907 1.00 53.95 C ATOM 1098 C GLY A 186 27.817 24.797 −15.992 1.00 50.83 C ATOM 1099 O GLY A 186 28.177 24.949 −14.837 1.00 50.90 O ATOM 1100 N LEU A 187 26.859 25.530 −16.522 1.00 47.72 N ATOM 1101 CA LEU A 187 26.072 26.384 −15.676 1.00 52.35 C ATOM 1102 CB LEU A 187 25.600 27.634 −16.431 1.00 53.00 C ATOM 1103 CG LEU A 187 24.775 27.624 −17.718 1.00 45.22 C ATOM 1104 CD1 LEU A 187 23.292 27.677 −17.413 1.00 50.82 C ATOM 1105 CD2 LEU A 187 25.183 28.833 −18.553 1.00 45.36 C ATOM 1106 C LEU A 187 24.922 25.529 −15.162 1.00 56.71 C ATOM 1107 O LEU A 187 24.288 24.805 −15.934 1.00 53.21 O ATOM 1108 N LEU A 188 24.672 25.611 −13.857 1.00 52.34 N ATOM 1109 CA LEU A 188 23.799 24.667 −13.160 1.00 54.15 C ATOM 1110 CB LEU A 188 24.305 24.446 −11.725 1.00 51.02 C ATOM 1111 CG LEU A 188 25.794 24.155 −11.523 1.00 54.04 C ATOM 1112 CD1 LEU A 188 26.560 25.421 −11.723 1.00 54.79 C ATOM 1113 CD2 LEU A 188 26.084 23.617 −10.124 1.00 51.54 C ATOM 1114 C LEU A 188 22.331 25.098 −13.112 1.00 51.19 C ATOM 1115 O LEU A 188 21.432 24.261 −12.963 1.00 49.46 O ATOM 1116 N ALA A 189 22.101 26.404 −13.207 1.00 47.21 N ATOM 1117 CA ALA A 189 20.765 26.961 −13.054 1.00 45.26 C ATOM 1118 CB ALA A 189 20.189 26.541 −11.731 1.00 47.46 C ATOM 1119 C ALA A 189 20.786 28.480 −13.155 1.00 46.31 C ATOM 1120 O ALA A 189 21.849 29.100 −13.154 1.00 46.78 O ATOM 1121 N HIS A 190 19.602 29.071 −13.245 1.00 47.54 N ATOM 1122 CA HIS A 190 19.457 30.518 −13.284 1.00 45.40 C ATOM 1123 CB HIS A 190 19.669 31.035 −14.686 1.00 46.58 C ATOM 1124 CG HIS A 190 18.770 30.395 −15.689 1.00 48.95 C ATOM 1125 CD2 HIS A 190 17.471 30.020 −15.602 1.00 46.62 C ATOM 1126 ND1 HIS A 190 19.197 30.024 −16.945 1.00 50.60 N ATOM 1127 CE1 HIS A 190 18.191 29.476 −17.601 1.00 54.86 C ATOM 1128 NE2 HIS A 190 17.136 29.451 −16.804 1.00 53.33 N ATOM 1129 C HIS A 190 18.046 30.861 −12.876 1.00 45.60 C ATOM 1130 O HIS A 190 17.288 29.981 −12.458 1.00 40.73 O ATOM 1131 N ALA A 191 17.685 32.132 −13.056 1.00 45.00 N ATOM 1132 CA ALA A 191 16.467 32.680 −12.467 1.00 45.71 C ATOM 1133 CB ALA A 191 16.546 32.557 −10.941 1.00 44.61 C ATOM 1134 C ALA A 191 16.281 34.147 −12.857 1.00 47.09 C ATOM 1135 O ALA A 191 17.248 34.884 −12.943 1.00 52.05 O ATOM 1136 N PHE A 192 15.041 34.577 −13.074 1.00 47.51 N ATOM 1137 CA PHE A 192 14.765 35.977 −13.398 1.00 46.69 C ATOM 1138 CB PHE A 192 13.613 36.088 −14.418 1.00 50.27 C ATOM 1139 CG PHE A 192 13.759 35.208 −15.646 1.00 44.25 C ATOM 1140 CD1 PHE A 192 14.260 35.719 −16.827 1.00 49.72 C ATOM 1141 CD2 PHE A 192 13.346 33.890 −15.627 1.00 48.08 C ATOM 1142 CE1 PHE A 192 14.381 34.925 −17.957 1.00 48.94 C ATOM 1143 CE2 PHE A 192 13.460 33.097 −16.756 1.00 51.61 C ATOM 1144 CZ PHE A 192 13.980 33.615 −17.922 1.00 45.92 C ATOM 1145 C PHE A 192 14.420 36.817 −12.135 1.00 52.44 C ATOM 1146 O PHE A 192 14.043 36.278 −11.082 1.00 50.67 O ATOM 1147 N PRO A 193 14.522 38.149 −12.245 1.00 51.08 N ATOM 1148 CD PRO A 193 14.872 38.912 −13.453 1.00 50.04 C ATOM 1149 CA PRO A 193 14.186 39.030 −11.117 1.00 53.51 C ATOM 1150 CB PRO A 193 14.710 40.407 −11.572 1.00 54.61 C ATOM 1151 CG PRO A 193 15.401 40.185 −12.887 1.00 53.64 C ATOM 1152 C PRO A 193 12.677 39.128 −10.898 1.00 53.09 C ATOM 1153 O PRO A 193 11.922 38.822 −11.822 1.00 50.49 O ATOM 1154 N PRO A 194 12.247 39.574 −9.698 1.00 59.93 N ATOM 1155 CD PRO A 194 13.170 39.901 −8.593 1.00 52.43 C ATOM 1156 CA PRO A 194 10.833 39.787 −9.317 1.00 53.62 C ATOM 1157 CB PRO A 194 10.939 40.606 −8.027 1.00 52.94 C ATOM 1158 CG PRO A 194 12.247 40.200 −7.430 1.00 48.93 C ATOM 1159 C PRO A 194 10.025 40.573 −10.346 1.00 54.51 C ATOM 1160 O PRO A 194 10.471 41.603 −10.853 1.00 57.29 O ATOM 1161 N GLY A 195 8.822 40.094 −10.637 1.00 56.71 N ATOM 1162 CA GLY A 195 7.976 40.747 −11.617 1.00 55.75 C ATOM 1163 C GLY A 195 6.883 39.838 −12.151 1.00 57.74 C ATOM 1164 O GLY A 195 6.694 38.705 −11.666 1.00 49.18 O ATOM 1165 N PRO A 196 6.163 40.324 −13.172 1.00 53.82 N ATOM 1166 CD PRO A 196 6.644 41.395 −14.058 1.00 52.78 C ATOM 1167 CA PRO A 196 5.003 39.634 −13.732 1.00 50.88 C ATOM 1168 CB PRO A 196 4.398 40.673 −14.682 1.00 58.96 C ATOM 1169 CG PRO A 196 5.415 41.810 −14.797 1.00 56.04 C ATOM 1170 C PRO A 196 5.466 38.463 −14.559 1.00 52.09 C ATOM 1171 O PRO A 196 6.599 38.456 −15.028 1.00 53.13 O ATOM 1172 N GLY A 197 4.592 37.487 −14.741 1.00 55.31 N ATOM 1173 CA GLY A 197 4.855 36.410 −15.666 1.00 47.45 C ATOM 1174 C GLY A 197 6.042 35.601 −15.239 1.00 46.08 C ATOM 1175 O GLY A 197 6.044 35.058 −14.157 1.00 47.42 O ATOM 1176 N ILE A 198 7.050 35.531 −16.101 1.00 53.53 N ATOM 1177 CA ILE A 198 8.191 34.649 −15.896 1.00 50.94 C ATOM 1178 CB ILE A 198 8.972 34.432 −17.229 1.00 51.79 C ATOM 1179 CG2 ILE A 198 9.782 35.659 −17.602 1.00 48.97 C ATOM 1180 CG1 ILE A 198 9.866 33.199 −17.147 1.00 50.21 C ATOM 1181 CD1 ILE A 198 10.385 32.741 −18.497 1.00 50.20 C ATOM 1182 C ILE A 198 9.112 35.212 −14.825 1.00 56.49 C ATOM 1183 O ILE A 198 9.738 34.469 −14.057 1.00 52.71 O ATOM 1184 N GLN A 199 9.177 36.536 −14.763 1.00 53.34 N ATOM 1185 CA GLN A 199 10.068 37.181 −13.819 1.00 54.53 C ATOM 1186 CB GLN A 199 9.852 38.695 −13.836 1.00 49.07 C ATOM 1187 CG GLN A 199 10.472 39.351 −15.062 1.00 47.73 C ATOM 1188 CD GLN A 199 10.253 40.847 −15.096 1.00 56.70 C ATOM 1189 OE1 GLN A 199 10.307 41.522 −14.062 1.00 60.68 O ATOM 1190 NE2 GLN A 199 10.000 41.379 −16.285 1.00 54.42 N ATOM 1191 C GLN A 199 9.940 36.559 −12.416 1.00 54.45 C ATOM 1192 O GLN A 199 8.852 36.467 −11.852 1.00 53.89 O ATOM 1193 N GLY A 200 11.061 36.088 −11.884 1.00 47.58 N ATOM 1194 CA GLY A 200 11.063 35.445 −10.585 1.00 50.84 C ATOM 1195 C GLY A 200 11.093 33.925 −10.596 1.00 44.43 C ATOM 1196 O GLY A 200 11.155 33.288 −9.551 1.00 50.23 O ATOM 1197 N ASP A 201 11.020 33.325 −11.767 1.00 45.65 N ATOM 1198 CA ASP A 201 11.118 31.875 −11.849 1.00 49.03 C ATOM 1199 CB ASP A 201 10.638 31.385 −13.216 1.00 47.76 C ATOM 1200 CG ASP A 201 9.190 31.731 −13.479 1.00 53.40 C ATOM 1201 OD1 ASP A 201 8.454 31.947 −12.478 1.00 48.96 O ATOM 1202 OD2 ASP A 201 8.799 31.792 −14.682 1.00 47.36 O ATOM 1203 C ASP A 201 12.556 31.414 −11.614 1.00 45.75 C ATOM 1204 O ASP A 201 13.511 32.178 −11.791 1.00 44.25 O ATOM 1205 N ALA A 202 12.707 30.156 −11.234 1.00 42.74 N ATOM 1206 CA ALA A 202 14.017 29.594 −10.988 1.00 42.72 C ATOM 1207 CB ALA A 202 14.258 29.447 −9.495 1.00 37.57 C ATOM 1208 C ALA A 202 14.130 28.260 −11.700 1.00 44.82 C ATOM 1209 O ALA A 202 13.297 27.372 −11.509 1.00 45.90 O ATOM 1210 N HIS A 203 15.161 28.127 −12.527 1.00 46.40 N ATOM 1211 CA HIS A 203 15.308 26.963 −13.388 1.00 46.58 C ATOM 1212 CB HIS A 203 15.354 27.385 −14.859 1.00 47.68 C ATOM 1213 CG HIS A 203 14.053 27.903 −15.385 1.00 54.88 C ATOM 1214 CD2 HIS A 203 12.775 27.673 −14.996 1.00 52.76 C ATOM 1215 ND1 HIS A 203 13.975 28.777 −16.447 1.00 57.89 N ATOM 1216 CE1 HIS A 203 12.711 29.065 −16.694 1.00 52.94 C ATOM 1217 NE2 HIS A 203 11.961 28.403 −15.830 1.00 54.03 N ATOM 1218 C HIS A 203 16.576 26.218 −13.042 1.00 48.67 C ATOM 1219 O HIS A 203 17.647 26.800 −12.958 1.00 49.53 O ATOM 1220 N PHE A 204 16.457 24.921 −12.832 1.00 49.15 N ATOM 1221 CA PHE A 204 17.631 24.132 −12.528 1.00 48.68 C ATOM 1222 CB PHE A 204 17.422 23.302 −11.256 1.00 49.78 C ATOM 1223 CG PHE A 204 17.237 24.137 −10.022 1.00 49.48 C ATOM 1224 CD1 PHE A 204 16.076 24.866 −9.834 1.00 46.13 C ATOM 1225 CD2 PHE A 204 18.224 24.197 −9.063 1.00 47.08 C ATOM 1226 CE1 PHE A 204 15.907 25.642 −8.721 1.00 48.78 C ATOM 1227 CE2 PHE A 204 18.051 24.959 −7.932 1.00 52.47 C ATOM 1228 CZ PHE A 204 16.891 25.685 −7.760 1.00 52.90 C ATOM 1229 C PHE A 204 17.854 23.223 −13.696 1.00 54.17 C ATOM 1230 O PHE A 204 16.895 22.763 −14.313 1.00 57.28 O ATOM 1231 N ASP A 205 19.117 22.958 −13.995 1.00 52.18 N ATOM 1232 CA ASP A 205 19.472 22.096 −15.111 1.00 52.75 C ATOM 1233 CB ASP A 205 20.793 22.557 −15.707 1.00 49.26 C ATOM 1234 CG ASP A 205 21.334 21.596 −16.701 1.00 53.77 C ATOM 1235 OD1 ASP A 205 20.547 20.771 −17.227 1.00 55.06 O ATOM 1236 OD2 ASP A 205 22.550 21.669 −16.958 1.00 55.12 O ATOM 1237 C ASP A 205 19.576 20.644 −14.662 1.00 52.89 C ATOM 1238 O ASP A 205 20.451 20.299 −13.867 1.00 48.54 O ATOM 1239 N ASP A 206 18.687 19.803 −15.190 1.00 53.62 N ATOM 1240 CA ASP A 206 18.602 18.399 −14.784 1.00 53.41 C ATOM 1241 CB ASP A 206 17.168 17.869 −14.940 1.00 52.21 C ATOM 1242 CG ASP A 206 16.868 16.693 −14.005 1.00 59.79 C ATOM 1243 OD1 ASP A 206 17.792 16.239 −13.280 1.00 55.02 O ATOM 1244 OD2 ASP A 206 15.701 16.234 −13.992 1.00 58.60 O ATOM 1245 C ASP A 206 19.593 17.443 −15.466 1.00 52.94 C ATOM 1246 O ASP A 206 19.596 16.256 −15.163 1.00 58.03 O ATOM 1247 N ASP A 207 20.419 17.931 −16.386 1.00 51.13 N ATOM 1248 CA ASP A 207 21.557 17.126 −16.835 1.00 52.04 C ATOM 1249 CB ASP A 207 22.303 17.803 −17.995 1.00 52.97 C ATOM 1250 CG ASP A 207 21.490 17.823 −19.305 1.00 56.40 C ATOM 1251 OD1 ASP A 207 20.828 16.811 −19.615 1.00 48.96 O ATOM 1252 OD2 ASP A 207 21.526 18.850 −20.029 1.00 53.87 O ATOM 1253 C ASP A 207 22.501 16.894 −15.640 1.00 56.25 C ATOM 1254 O ASP A 207 23.274 15.935 −15.611 1.00 55.10 O ATOM 1255 N GLU A 208 22.403 17.765 −14.637 1.00 54.18 N ATOM 1256 CA GLU A 208 23.293 17.707 −13.485 1.00 53.04 C ATOM 1257 CB GLU A 208 23.225 19.012 −12.716 1.00 54.88 C ATOM 1258 CG GLU A 208 23.728 20.152 −13.513 1.00 54.89 C ATOM 1259 CD GLU A 208 25.110 19.873 −14.046 1.00 54.46 C ATOM 1260 OE1 GLU A 208 25.762 18.913 −13.578 1.00 49.20 O ATOM 1261 OE2 GLU A 208 25.542 20.618 −14.931 1.00 56.58 O ATOM 1262 C GLU A 208 22.995 16.576 −12.535 1.00 51.63 C ATOM 1263 O GLU A 208 22.000 15.883 −12.681 1.00 58.04 O ATOM 1264 N LEU A 209 23.866 16.405 −11.549 1.00 50.40 N ATOM 1265 CA LEU A 209 23.633 15.434 −10.486 1.00 50.87 C ATOM 1266 CB LEU A 209 24.855 14.548 −10.287 1.00 51.43 C ATOM 1267 CG LEU A 209 24.706 13.513 −9.170 1.00 49.42 C ATOM 1268 CD1 LEU A 209 23.547 12.569 −9.459 1.00 39.99 C ATOM 1269 CD2 LEU A 209 26.019 12.744 −8.968 1.00 48.33 C ATOM 1270 C LEU A 209 23.273 16.112 −9.166 1.00 58.35 C ATOM 1271 O LEU A 209 24.154 16.517 −8.397 1.00 58.84 O ATOM 1272 N TRP A 210 21.976 16.234 −8.898 1.00 54.16 N ATOM 1273 CA TRP A 210 21.538 16.883 −7.668 1.00 53.85 C ATOM 1274 CB TRP A 210 20.113 17.430 −7.815 1.00 52.39 C ATOM 1275 CG TRP A 210 20.022 18.458 −8.861 1.00 51.73 C ATOM 1276 CD2 TRP A 210 20.601 19.759 −8.820 1.00 49.71 C ATOM 1277 CE2 TRP A 210 20.303 20.390 −10.041 1.00 53.20 C ATOM 1278 CE3 TRP A 210 21.343 20.455 −7.866 1.00 55.71 C ATOM 1279 CD1 TRP A 210 19.411 18.346 −10.077 1.00 59.25 C ATOM 1280 NE1 TRP A 210 19.571 19.510 −10.793 1.00 56.99 N ATOM 1281 CZ2 TRP A 210 20.706 21.686 −10.326 1.00 52.95 C ATOM 1282 CZ3 TRP A 210 21.751 21.747 −8.161 1.00 54.32 C ATOM 1283 CH2 TRP A 210 21.433 22.342 −9.380 1.00 47.47 C ATOM 1284 C TRP A 210 21.604 15.926 −6.491 1.00 55.36 C ATOM 1285 O TRP A 210 20.939 14.889 −6.484 1.00 58.86 O ATOM 1286 N SER A 211 22.420 16.267 −5.501 1.00 58.89 N ATOM 1287 CA SER A 211 22.329 15.610 −4.198 1.00 53.76 C ATOM 1288 CB SER A 211 23.497 14.656 −3.944 1.00 53.66 C ATOM 1289 OG SER A 211 24.739 15.268 −4.231 1.00 61.99 O ATOM 1290 C SER A 211 22.274 16.681 −3.134 1.00 55.16 C ATOM 1291 O SER A 211 22.223 17.865 −3.445 1.00 57.63 O ATOM 1292 N LEU A 212 22.266 16.275 −1.875 1.00 56.60 N ATOM 1293 CA LEU A 212 22.243 17.253 −0.810 1.00 54.90 C ATOM 1294 CB LEU A 212 21.029 17.050 0.106 1.00 58.38 C ATOM 1295 CG LEU A 212 19.683 17.481 −0.500 1.00 58.24 C ATOM 1296 CD1 LEU A 212 18.584 17.474 0.557 1.00 51.11 C ATOM 1297 CD2 LEU A 212 19.755 18.861 −1.163 1.00 48.49 C ATOM 1298 C LEU A 212 23.549 17.260 −0.031 1.00 53.64 C ATOM 1299 O LEU A 212 23.873 18.259 0.618 1.00 56.42 O ATOM 1300 N GLY A 213 24.315 16.169 −0.123 1.00 52.37 N ATOM 1301 CA GLY A 213 25.583 16.064 0.598 1.00 62.80 C ATOM 1302 C GLY A 213 26.828 15.846 −0.249 1.00 62.66 C ATOM 1303 O GLY A 213 27.775 15.160 0.164 1.00 59.90 O ATOM 1304 O ALA A 393 23.210 18.572 −5.818 1.00 20.00 O ATOM 1305 N ALA A 393 25.435 20.059 −7.947 1.00 20.00 N ATOM 1306 CA ALA A 393 25.149 18.932 −7.088 1.00 20.00 C ATOM 1307 C ALA A 393 24.211 19.225 −5.924 1.00 20.00 C ATOM 1308 CB ALA A 393 26.407 18.306 −6.613 1.00 20.00 C ATOM 1309 N SER A 394 24.505 20.173 −5.043 1.00 45.74 N ATOM 1310 CA SER A 394 23.603 20.483 −3.916 1.00 51.63 C ATOM 1311 CB SER A 394 24.337 21.279 −2.871 1.00 45.02 C ATOM 1312 OG SER A 394 23.524 21.451 −1.753 1.00 48.07 O ATOM 1313 C SER A 394 22.350 21.256 −4.269 1.00 47.42 C ATOM 1314 O SER A 394 22.453 22.376 −4.643 1.00 43.55 O ATOM 1315 N LEU A 395 21.171 20.665 −4.157 1.00 48.81 N ATOM 1316 CA LEU A 395 19.953 21.315 −4.618 1.00 49.07 C ATOM 1317 CB LEU A 395 18.819 20.304 −4.790 1.00 45.13 C ATOM 1318 CG LEU A 395 17.497 20.934 −5.220 1.00 51.30 C ATOM 1319 CD1 LEU A 395 17.720 21.769 −6.475 1.00 49.01 C ATOM 1320 CD2 LEU A 395 16.420 19.877 −5.446 1.00 52.96 C ATOM 1321 C LEU A 395 19.584 22.389 −3.607 1.00 48.37 C ATOM 1322 O LEU A 395 18.940 23.383 −3.931 1.00 47.35 O ATOM 1323 N PHE A 396 20.031 22.184 −2.376 1.00 45.96 N ATOM 1324 CA PHE A 396 19.818 23.149 −1.319 1.00 44.23 C ATOM 1325 CB PHE A 396 20.205 22.540 0.025 1.00 44.30 C ATOM 1326 CG PHE A 396 20.103 23.502 1.172 1.00 45.81 C ATOM 1327 CD1 PHE A 396 18.946 24.253 1.355 1.00 38.27 C ATOM 1328 CD2 PHE A 396 21.161 23.650 2.074 1.00 40.08 C ATOM 1329 CE1 PHE A 396 18.841 25.135 2.398 1.00 38.81 C ATOM 1330 CE2 PHE A 396 21.062 24.534 3.126 1.00 40.86 C ATOM 1331 CZ PHE A 396 19.897 25.281 3.293 1.00 41.25 C ATOM 1332 C PHE A 396 20.584 24.451 −1.570 1.00 42.14 C ATOM 1333 O PHE A 396 19.983 25.504 −1.796 1.00 45.93 O ATOM 1334 N LEU A 397 21.907 24.376 −1.538 1.00 43.02 N ATOM 1335 CA LEU A 397 22.741 25.567 −1.695 1.00 43.37 C ATOM 1336 CB LEU A 397 24.218 25.178 −1.734 1.00 44.70 C ATOM 1337 CG LEU A 397 24.781 24.463 −0.511 1.00 45.60 C ATOM 1338 CD1 LEU A 397 26.267 24.158 −0.696 1.00 51.63 C ATOM 1339 CD2 LEU A 397 24.547 25.316 0.715 1.00 41.22 C ATOM 1340 C LEU A 397 22.386 26.324 −2.962 1.00 39.74 C ATOM 1341 O LEU A 397 22.189 27.535 −2.933 1.00 35.91 O ATOM 1342 N VAL A 398 22.334 25.604 −4.085 1.00 43.48 N ATOM 1343 CA VAL A 398 21.978 26.215 −5.366 1.00 41.45 C ATOM 1344 CB VAL A 398 21.921 25.192 −6.513 1.00 45.15 C ATOM 1345 CG1 VAL A 398 21.399 25.856 −7.769 1.00 45.91 C ATOM 1346 CG2 VAL A 398 23.300 24.586 −6.769 1.00 45.64 C ATOM 1347 C VAL A 398 20.636 26.944 −5.284 1.00 42.18 C ATOM 1348 O VAL A 398 20.541 28.116 −5.630 1.00 44.42 O ATOM 1349 N ALA A 399 19.609 26.248 −4.815 1.00 37.38 N ATOM 1350 CA ALA A 399 18.281 26.834 −4.692 1.00 44.07 C ATOM 1351 CB ALA A 399 17.328 25.842 −4.060 1.00 43.49 C ATOM 1352 C ALA A 399 18.285 28.135 −3.895 1.00 44.78 C ATOM 1353 O ALA A 399 17.612 29.105 −4.259 1.00 41.31 O ATOM 1354 N ALA A 400 19.034 28.151 −2.798 1.00 40.10 N ATOM 1355 CA ALA A 400 19.085 29.328 −1.956 1.00 41.10 C ATOM 1356 CB ALA A 400 19.949 29.074 −0.724 1.00 40.45 C ATOM 1357 C ALA A 400 19.618 30.498 −2.769 1.00 43.50 C ATOM 1358 O ALA A 400 19.033 31.587 −2.775 1.00 46.11 O ATOM 1359 N HIS A 401 20.712 30.252 −3.484 1.00 40.98 N ATOM 1360 CA HIS A 401 21.345 31.265 −4.317 1.00 43.01 C ATOM 1361 CB HIS A 401 22.617 30.675 −4.909 1.00 38.92 C ATOM 1362 CG HIS A 401 23.296 31.556 −5.906 1.00 41.73 C ATOM 1363 CD2 HIS A 401 23.076 31.728 −7.235 1.00 44.23 C ATOM 1364 ND1 HIS A 401 24.369 32.354 −5.584 1.00 39.07 N ATOM 1365 CE1 HIS A 401 24.765 33.005 −6.663 1.00 46.09 C ATOM 1366 NE2 HIS A 401 23.999 32.642 −7.681 1.00 40.63 N ATOM 1367 C HIS A 401 20.414 31.813 −5.415 1.00 43.12 C ATOM 1368 O HIS A 401 20.371 33.020 −5.654 1.00 43.14 O ATOM 1369 N GLU A 402 19.657 30.931 −6.064 1.00 43.68 N ATOM 1370 CA GLU A 402 18.701 31.349 −7.104 1.00 47.19 C ATOM 1371 CB GLU A 402 18.241 30.144 −7.940 1.00 43.29 C ATOM 1372 CG GLU A 402 19.382 29.302 −8.525 1.00 40.69 C ATOM 1373 CD GLU A 402 20.130 30.016 −9.639 1.00 48.11 C ATOM 1374 OE1 GLU A 402 21.122 29.450 −10.170 1.00 40.42 O ATOM 1375 OE2 GLU A 402 19.717 31.146 −9.987 1.00 48.18 O ATOM 1376 C GLU A 402 17.487 32.094 −6.522 1.00 43.44 C ATOM 1377 O GLU A 402 16.944 33.002 −7.147 1.00 37.75 O ATOM 1378 N PHE A 403 17.078 31.715 −5.316 1.00 41.53 N ATOM 1379 CA PHE A 403 15.947 32.360 −4.680 1.00 39.12 C ATOM 1380 CB PHE A 403 15.511 31.580 −3.445 1.00 39.28 C ATOM 1381 CG PHE A 403 14.961 30.224 −3.752 1.00 39.09 C ATOM 1382 CD1 PHE A 403 14.761 29.823 −5.061 1.00 40.95 C ATOM 1383 CD2 PHE A 403 14.629 29.346 −2.727 1.00 47.14 C ATOM 1384 CE1 PHE A 403 14.243 28.571 −5.345 1.00 44.64 C ATOM 1385 CE2 PHE A 403 14.111 28.081 −2.996 1.00 45.88 C ATOM 1386 CZ PHE A 403 13.921 27.692 −4.299 1.00 48.91 C ATOM 1387 C PHE A 403 16.338 33.784 −4.324 1.00 45.90 C ATOM 1388 O PHE A 403 15.514 34.705 −4.379 1.00 43.30 O ATOM 1389 N GLY A 404 17.610 33.961 −3.969 1.00 46.50 N ATOM 1390 CA GLY A 404 18.174 35.287 −3.798 1.00 46.49 C ATOM 1391 C GLY A 404 17.957 36.102 −5.060 1.00 45.07 C ATOM 1392 O GLY A 404 17.574 37.268 −5.006 1.00 47.36 O ATOM 1393 N HIS A 405 18.189 35.478 −6.205 1.00 44.78 N ATOM 1394 CA HIS A 405 17.898 36.112 −7.491 1.00 45.23 C ATOM 1395 CB HIS A 405 18.324 35.209 −8.642 1.00 40.84 C ATOM 1396 CG HIS A 405 19.786 35.249 −8.932 1.00 44.94 C ATOM 1397 CD2 HIS A 405 20.623 34.315 −9.438 1.00 43.23 C ATOM 1398 ND1 HIS A 405 20.553 36.375 −8.718 1.00 48.52 N ATOM 1399 CE1 HIS A 405 21.803 36.125 −9.065 1.00 47.56 C ATOM 1400 NE2 HIS A 405 21.872 34.883 −9.510 1.00 45.91 N ATOM 1401 C HIS A 405 16.413 36.417 −7.632 1.00 48.50 C ATOM 1402 O HIS A 405 16.034 37.504 −8.079 1.00 48.44 O ATOM 1403 N ALA A 406 15.582 35.447 −7.250 1.00 45.85 N ATOM 1404 CA ALA A 406 14.134 35.553 −7.404 1.00 45.01 C ATOM 1405 CB ALA A 406 13.467 34.185 −7.215 1.00 43.56 C ATOM 1406 C ALA A 406 13.543 36.570 −6.444 1.00 48.01 C ATOM 1407 O ALA A 406 12.327 36.695 −6.338 1.00 47.67 O ATOM 1408 N LEU A 407 14.406 37.282 −5.728 1.00 49.18 N ATOM 1409 CA LEU A 407 13.942 38.343 −4.843 1.00 45.44 C ATOM 1410 CB LEU A 407 14.226 38.001 −3.379 1.00 44.39 C ATOM 1411 CG LEU A 407 13.660 36.654 −2.927 1.00 44.73 C ATOM 1412 CD1 LEU A 407 13.728 36.501 −1.424 1.00 36.77 C ATOM 1413 CD2 LEU A 407 12.243 36.500 −3.383 1.00 47.55 C ATOM 1414 C LEU A 407 14.562 39.692 −5.218 1.00 47.20 C ATOM 1415 O LEU A 407 14.140 40.718 −4.713 1.00 52.35 O ATOM 1416 N GLY A 408 15.556 39.696 −6.106 1.00 43.70 N ATOM 1417 CA GLY A 408 16.163 40.939 −6.554 1.00 41.72 C ATOM 1418 C GLY A 408 17.665 41.014 −6.351 1.00 51.56 C ATOM 1419 O GLY A 408 18.299 42.013 −6.686 1.00 50.41 O ATOM 1420 N LEU A 409 18.245 39.953 −5.803 1.00 51.53 N ATOM 1421 CA LEU A 409 19.683 39.928 −5.561 1.00 53.22 C ATOM 1422 CB LEU A 409 20.030 38.963 −4.421 1.00 51.23 C ATOM 1423 CG LEU A 409 19.477 39.259 −3.022 1.00 52.31 C ATOM 1424 CD1 LEU A 409 20.182 38.387 −1.999 1.00 46.17 C ATOM 1425 CD2 LEU A 409 19.632 40.735 −2.659 1.00 48.56 C ATOM 1426 C LEU A 409 20.487 39.559 −6.809 1.00 54.16 C ATOM 1427 O LEU A 409 20.382 38.437 −7.307 1.00 54.30 O ATOM 1428 N ASP A 410 21.293 40.493 −7.308 1.00 52.06 N ATOM 1429 CA ASP A 410 22.279 40.148 −8.333 1.00 54.31 C ATOM 1430 CB ASP A 410 22.765 41.387 −9.099 1.00 55.59 C ATOM 1431 CG ASP A 410 23.166 42.519 −8.184 1.00 59.15 C ATOM 1432 OD1 ASP A 410 23.728 43.523 −8.688 1.00 54.50 O ATOM 1433 OD2 ASP A 410 22.906 42.405 −6.961 1.00 61.03 O ATOM 1434 C ASP A 410 23.453 39.397 −7.698 1.00 50.52 C ATOM 1435 O ASP A 410 23.286 38.710 −6.691 1.00 50.53 O ATOM 1436 N HIS A 411 24.643 39.523 −8.275 1.00 49.09 N ATOM 1437 CA HIS A 411 25.749 38.703 −7.807 1.00 44.99 C ATOM 1438 CB HIS A 411 26.591 38.183 −8.959 1.00 40.09 C ATOM 1439 CG HIS A 411 26.067 36.917 −9.550 1.00 44.17 C ATOM 1440 CD2 HIS A 411 25.485 35.843 −8.968 1.00 42.50 C ATOM 1441 ND1 HIS A 411 26.100 36.650 −10.903 1.00 45.00 N ATOM 1442 CE1 HIS A 411 25.566 35.465 −11.128 1.00 42.71 C ATOM 1443 NE2 HIS A 411 25.177 34.960 −9.971 1.00 45.55 N ATOM 1444 C HIS A 411 26.620 39.421 −6.810 1.00 44.48 C ATOM 1445 O HIS A 411 26.749 40.641 −6.856 1.00 50.53 O ATOM 1446 N SER A 412 27.203 38.659 −5.894 1.00 35.99 N ATOM 1447 CA SER A 412 28.255 39.196 −5.039 1.00 41.02 C ATOM 1448 CB SER A 412 28.128 38.650 −3.631 1.00 43.53 C ATOM 1449 OG SER A 412 29.377 38.710 −2.985 1.00 44.46 O ATOM 1450 C SER A 412 29.663 38.895 −5.571 1.00 41.96 C ATOM 1451 O SER A 412 29.874 37.948 −6.332 1.00 43.62 O ATOM 1452 N SER A 413 30.620 39.711 −5.143 1.00 47.75 N ATOM 1453 CA SER A 413 32.019 39.546 −5.517 1.00 41.57 C ATOM 1454 CB SER A 413 32.576 40.857 −6.079 1.00 45.15 C ATOM 1455 OG SER A 413 31.879 41.251 −7.269 1.00 49.36 O ATOM 1456 C SER A 413 32.831 39.050 −4.318 1.00 45.13 C ATOM 1457 O SER A 413 34.002 38.655 −4.454 1.00 41.95 O ATOM 1458 N VAL A 414 32.191 39.056 −3.144 1.00 38.89 N ATOM 1459 CA VAL A 414 32.760 38.420 −1.961 1.00 39.07 C ATOM 1460 CB VAL A 414 31.897 38.658 −0.691 1.00 37.42 C ATOM 1461 CG1 VAL A 414 32.604 38.155 0.526 1.00 40.27 C ATOM 1462 CG2 VAL A 414 31.568 40.109 −0.510 1.00 33.45 C ATOM 1463 C VAL A 414 32.752 36.920 −2.225 1.00 43.72 C ATOM 1464 O VAL A 414 31.675 36.315 −2.252 1.00 44.14 O ATOM 1465 N PRO A 415 33.941 36.299 −2.372 1.00 42.29 N ATOM 1466 CD PRO A 415 35.275 36.862 −2.092 1.00 45.11 C ATOM 1467 CA PRO A 415 34.018 34.882 −2.770 1.00 45.06 C ATOM 1468 CB PRO A 415 35.523 34.570 −2.734 1.00 47.73 C ATOM 1469 CG PRO A 415 36.196 35.899 −2.816 1.00 50.28 C ATOM 1470 C PRO A 415 33.242 33.891 −1.886 1.00 47.68 C ATOM 1471 O PRO A 415 32.822 32.844 −2.389 1.00 52.28 O ATOM 1472 N GLU A 416 33.042 34.191 −0.607 1.00 45.64 N ATOM 1473 CA GLU A 416 32.297 33.257 0.244 1.00 40.43 C ATOM 1474 CB GLU A 416 32.860 33.229 1.667 1.00 42.18 C ATOM 1475 CG GLU A 416 34.376 33.415 1.756 1.00 53.36 C ATOM 1476 CD GLU A 416 34.788 34.883 1.751 1.00 56.65 C ATOM 1477 OE1 GLU A 416 35.535 35.284 0.836 1.00 50.58 O ATOM 1478 OE2 GLU A 416 34.354 35.637 2.657 1.00 58.81 O ATOM 1479 C GLU A 416 30.791 33.552 0.262 1.00 43.70 C ATOM 1480 O GLU A 416 29.995 32.714 0.677 1.00 38.87 O ATOM 1481 N ALA A 417 30.400 34.735 −0.205 1.00 46.04 N ATOM 1482 CA ALA A 417 28.985 35.093 −0.242 1.00 47.70 C ATOM 1483 CB ALA A 417 28.791 36.472 −0.867 1.00 41.04 C ATOM 1484 C ALA A 417 28.193 34.047 −1.010 1.00 47.56 C ATOM 1485 O ALA A 417 28.671 33.534 −2.018 1.00 39.78 O ATOM 1486 N LEU A 418 26.986 33.735 −0.532 1.00 44.74 N ATOM 1487 CA LEU A 418 26.121 32.783 −1.225 1.00 42.49 C ATOM 1488 CB LEU A 418 24.800 32.586 −0.466 1.00 44.08 C ATOM 1489 CG LEU A 418 23.716 31.749 −1.171 1.00 42.99 C ATOM 1490 CD1 LEU A 418 24.155 30.320 −1.365 1.00 36.84 C ATOM 1491 CD2 LEU A 418 22.418 31.767 −0.391 1.00 44.69 C ATOM 1492 C LEU A 418 25.835 33.254 −2.657 1.00 43.93 C ATOM 1493 O LEU A 418 25.603 32.436 −3.539 1.00 39.69 O ATOM 1494 N MET A 419 25.846 34.572 −2.876 1.00 44.25 N ATOM 1495 CA MET A 419 25.506 35.126 −4.187 1.00 44.65 C ATOM 1496 CB MET A 419 24.845 36.500 −4.087 1.00 40.96 C ATOM 1497 CG MET A 419 23.449 36.456 −3.486 1.00 44.77 C ATOM 1498 SD MET A 419 22.400 35.063 −3.977 1.00 40.90 S ATOM 1499 CE MET A 419 21.580 35.762 −5.417 1.00 46.71 C ATOM 1500 C MET A 419 26.700 35.198 −5.114 1.00 50.22 C ATOM 1501 O MET A 419 26.603 35.734 −6.227 1.00 47.11 O ATOM 1502 N TYR A 420 27.833 34.675 −4.646 1.00 49.40 N ATOM 1503 CA TYR A 420 28.975 34.483 −5.525 1.00 46.15 C ATOM 1504 CB TYR A 420 30.164 33.897 −4.767 1.00 39.25 C ATOM 1505 CG TYR A 420 31.477 34.166 −5.443 1.00 46.65 C ATOM 1506 CD1 TYR A 420 31.885 35.472 −5.719 1.00 45.71 C ATOM 1507 CE1 TYR A 420 33.093 35.722 −6.349 1.00 43.70 C ATOM 1508 CD2 TYR A 420 32.316 33.121 −5.814 1.00 44.36 C ATOM 1509 CE2 TYR A 420 33.530 33.365 −6.436 1.00 43.93 C ATOM 1510 CZ TYR A 420 33.913 34.666 −6.706 1.00 43.91 C ATOM 1511 OH TYR A 420 35.127 34.902 −7.339 1.00 49.08 O ATOM 1512 C TYR A 420 28.523 33.539 −6.641 1.00 47.87 C ATOM 1513 O TYR A 420 27.847 32.535 −6.365 1.00 41.13 O ATOM 1514 N PRO A 421 28.884 33.868 −7.899 1.00 45.06 N ATOM 1515 CD PRO A 421 29.830 34.955 −8.199 1.00 47.69 C ATOM 1516 CA PRO A 421 28.490 33.142 −9.109 1.00 39.96 C ATOM 1517 CB PRO A 421 29.335 33.788 −10.207 1.00 40.80 C ATOM 1518 CG PRO A 421 29.684 35.118 −9.696 1.00 47.40 C ATOM 1519 C PRO A 421 28.845 31.673 −9.019 1.00 39.82 C ATOM 1520 O PRO A 421 28.011 30.820 −9.319 1.00 45.20 O ATOM 1521 N MET A 422 30.069 31.382 −8.605 1.00 40.21 N ATOM 1522 CA MET A 422 30.573 30.014 −8.651 1.00 43.33 C ATOM 1523 CB MET A 422 32.099 29.987 −8.608 1.00 35.61 C ATOM 1524 CG MET A 422 32.759 31.130 −9.313 1.00 36.89 C ATOM 1525 SD MET A 422 34.543 30.882 −9.282 1.00 50.38 S ATOM 1526 CE MET A 422 34.776 30.296 −7.613 1.00 52.91 C ATOM 1527 C MET A 422 30.031 29.127 −7.542 1.00 44.93 C ATOM 1528 O MET A 422 29.760 29.590 −6.423 1.00 37.87 O ATOM 1529 N TYR A 423 29.931 27.845 −7.836 1.00 47.07 N ATOM 1530 CA TYR A 423 29.474 26.847 −6.883 1.00 49.47 C ATOM 1531 CB TYR A 423 28.934 25.617 −7.637 1.00 44.82 C ATOM 1532 CG TYR A 423 28.490 24.499 −6.748 1.00 44.32 C ATOM 1533 CD1 TYR A 423 29.269 23.418 −6.544 1.00 43.33 C ATOM 1534 CE1 TYR A 423 28.890 22.443 −5.727 1.00 47.51 C ATOM 1535 CD2 TYR A 423 27.314 24.551 −6.095 1.00 44.64 C ATOM 1536 CE2 TYR A 423 26.936 23.582 −5.276 1.00 51.10 C ATOM 1537 CZ TYR A 423 27.723 22.530 −5.094 1.00 51.96 C ATOM 1538 OH TYR A 423 27.331 21.550 −4.266 1.00 53.25 O ATOM 1539 C TYR A 423 30.557 26.485 −5.850 1.00 53.41 C ATOM 1540 O TYR A 423 31.669 26.164 −6.189 1.00 57.20 O ATOM 1541 N ARG A 424 30.218 26.564 −4.577 1.00 52.95 N ATOM 1542 CA ARG A 424 31.138 26.277 −3.496 1.00 57.51 C ATOM 1543 CB ARG A 424 31.431 27.571 −2.744 1.00 67.76 C ATOM 1544 CG ARG A 424 30.369 27.952 −1.633 1.00 79.56 C ATOM 1545 CD ARG A 424 29.288 29.071 −2.008 1.00 81.71 C ATOM 1546 NE ARG A 424 28.344 28.724 −3.102 1.00 91.27 N ATOM 1547 CZ ARG A 424 27.187 28.091 −2.952 1.00 94.43 C ATOM 1548 NH1 ARG A 424 26.804 27.731 −1.755 1.00 88.26 N ATOM 1549 NH2 ARG A 424 26.420 27.824 −3.989 1.00 87.21 N ATOM 1550 C ARG A 424 30.393 25.424 −2.548 1.00 58.53 C ATOM 1551 O ARG A 424 29.453 25.877 −2.005 1.00 63.27 O ATOM 1552 N PHE A 425 30.768 24.185 −2.326 1.00 56.35 N ATOM 1553 CA PHE A 425 30.015 23.408 −1.369 1.00 55.76 C ATOM 1554 CB PHE A 425 30.055 21.920 −1.686 1.00 49.34 C ATOM 1555 CG PHE A 425 29.442 21.080 −0.630 1.00 51.59 C ATOM 1556 CD1 PHE A 425 28.098 20.882 −0.586 1.00 51.14 C ATOM 1557 CD2 PHE A 425 30.200 20.512 0.334 1.00 51.54 C ATOM 1558 CE1 PHE A 425 27.539 20.152 0.388 1.00 55.19 C ATOM 1559 CE2 PHE A 425 29.632 19.778 1.297 1.00 51.23 C ATOM 1560 CZ PHE A 425 28.299 19.608 1.324 1.00 55.45 C ATOM 1561 C PHE A 425 30.515 23.664 0.025 1.00 56.54 C ATOM 1562 O PHE A 425 31.662 23.462 0.317 1.00 58.86 O ATOM 1563 N THR A 426 29.648 24.150 0.883 1.00 49.43 N ATOM 1564 CA THR A 426 29.984 24.214 2.300 1.00 49.12 C ATOM 1565 CB THR A 426 29.851 25.636 2.884 1.00 48.52 C ATOM 1566 OG1 THR A 426 28.908 26.395 2.115 1.00 38.32 O ATOM 1567 CG2 THR A 426 31.211 26.345 2.948 1.00 51.03 C ATOM 1568 C THR A 426 29.062 23.344 3.130 1.00 51.69 C ATOM 1569 O THR A 426 28.023 22.878 2.666 1.00 57.10 O ATOM 1570 N GLU A 427 29.445 23.146 4.382 1.00 55.18 N ATOM 1571 CA GLU A 427 28.548 22.560 5.358 1.00 48.84 C ATOM 1572 CB GLU A 427 29.282 21.488 6.136 1.00 52.05 C ATOM 1573 CG GLU A 427 29.761 20.380 5.259 1.00 59.43 C ATOM 1574 CD GLU A 427 29.319 19.054 5.786 1.00 66.49 C ATOM 1575 OE1 GLU A 427 28.635 18.308 5.042 1.00 64.41 O ATOM 1576 OE2 GLU A 427 29.640 18.782 6.964 1.00 66.87 O ATOM 1577 C GLU A 427 28.073 23.669 6.286 1.00 43.30 C ATOM 1578 O GLU A 427 27.211 23.463 7.141 1.00 40.52 O ATOM 1579 N GLY A 428 28.637 24.858 6.085 1.00 45.34 N ATOM 1580 CA GLY A 428 28.368 25.990 6.954 1.00 44.83 C ATOM 1581 C GLY A 428 27.153 26.804 6.576 1.00 40.75 C ATOM 1582 O GLY A 428 26.628 26.689 5.454 1.00 39.15 O ATOM 1583 N PRO A 429 26.695 27.649 7.512 1.00 41.92 N ATOM 1584 CD PRO A 429 27.244 27.873 8.860 1.00 40.56 C ATOM 1585 CA PRO A 429 25.536 28.506 7.230 1.00 40.32 C ATOM 1586 CB PRO A 429 25.517 29.479 8.413 1.00 38.23 C ATOM 1587 CG PRO A 429 26.169 28.709 9.526 1.00 38.10 C ATOM 1588 C PRO A 429 25.765 29.235 5.912 1.00 42.90 C ATOM 1589 O PRO A 429 26.716 29.999 5.803 1.00 42.60 O ATOM 1590 N PRO A 430 24.899 28.979 4.919 1.00 41.39 N ATOM 1591 CD PRO A 430 23.692 28.147 5.091 1.00 37.51 C ATOM 1592 CA PRO A 430 25.033 29.482 3.549 1.00 38.22 C ATOM 1593 CB PRO A 430 23.752 28.979 2.856 1.00 39.94 C ATOM 1594 CG PRO A 430 23.331 27.789 3.669 1.00 50.66 C ATOM 1595 C PRO A 430 25.130 31.004 3.468 1.00 41.99 C ATOM 1596 O PRO A 430 25.955 31.540 2.710 1.00 43.61 O ATOM 1597 N LEU A 431 24.295 31.705 4.226 1.00 40.62 N ATOM 1598 CA LEU A 431 24.316 33.161 4.156 1.00 40.86 C ATOM 1599 CB LEU A 431 23.070 33.774 4.781 1.00 37.06 C ATOM 1600 CG LEU A 431 21.782 33.392 4.048 1.00 43.42 C ATOM 1601 CD1 LEU A 431 20.546 33.798 4.870 1.00 32.77 C ATOM 1602 CD2 LEU A 431 21.731 33.957 2.617 1.00 33.88 C ATOM 1603 C LEU A 431 25.586 33.774 4.749 1.00 42.26 C ATOM 1604 O LEU A 431 26.273 33.179 5.577 1.00 39.50 O ATOM 1605 N HIS A 432 25.939 34.924 4.201 1.00 41.64 N ATOM 1606 CA HIS A 432 26.995 35.770 4.691 1.00 47.91 C ATOM 1607 CB HIS A 432 28.235 35.676 3.832 1.00 45.37 C ATOM 1608 CG HIS A 432 28.913 34.357 3.923 1.00 55.67 C ATOM 1609 CD2 HIS A 432 28.627 33.179 3.343 1.00 58.20 C ATOM 1610 ND1 HIS A 432 30.017 34.139 4.702 1.00 67.58 N ATOM 1611 CE1 HIS A 432 30.384 32.884 4.594 1.00 66.58 C ATOM 1612 NE2 HIS A 432 29.563 32.284 3.766 1.00 63.94 N ATOM 1613 C HIS A 432 26.499 37.187 4.735 1.00 45.33 C ATOM 1614 O HIS A 432 25.458 37.486 4.231 1.00 38.00 O ATOM 1615 N LYS A 433 27.251 38.061 5.365 1.00 50.54 N ATOM 1616 CA LYS A 433 26.705 39.395 5.630 1.00 45.92 C ATOM 1617 CB LYS A 433 27.481 40.096 6.747 1.00 42.92 C ATOM 1618 CG LYS A 433 28.964 40.101 6.555 1.00 49.67 C ATOM 1619 CD LYS A 433 29.611 40.482 7.859 1.00 52.67 C ATOM 1620 CE LYS A 433 31.107 40.267 7.859 1.00 57.25 C ATOM 1621 NZ LYS A 433 31.623 40.785 9.151 1.00 52.97 N ATOM 1622 C LYS A 433 26.558 40.315 4.420 1.00 43.22 C ATOM 1623 O LYS A 433 25.932 41.360 4.543 1.00 43.46 O ATOM 1624 N ASP A 434 27.122 39.940 3.271 1.00 44.72 N ATOM 1625 CA ASP A 434 26.905 40.689 2.014 1.00 45.48 C ATOM 1626 CB ASP A 434 28.074 40.498 1.032 1.00 42.84 C ATOM 1627 CG ASP A 434 27.928 41.343 −0.252 1.00 44.04 C ATOM 1628 OD1 ASP A 434 28.099 42.582 −0.183 1.00 41.46 O ATOM 1629 OD2 ASP A 434 27.660 40.770 −1.336 1.00 38.31 O ATOM 1630 C ASP A 434 25.594 40.286 1.335 1.00 43.67 C ATOM 1631 O ASP A 434 24.973 41.092 0.652 1.00 42.15 O ATOM 1632 N ASP A 435 25.200 39.026 1.501 1.00 44.58 N ATOM 1633 CA ASP A 435 23.889 38.575 1.052 1.00 45.58 C ATOM 1634 CB ASP A 435 23.722 37.071 1.250 1.00 39.87 C ATOM 1635 CG ASP A 435 24.860 36.275 0.656 1.00 46.73 C ATOM 1636 OD1 ASP A 435 25.037 36.295 −0.582 1.00 45.92 O ATOM 1637 OD2 ASP A 435 25.570 35.611 1.431 1.00 47.44 O ATOM 1638 C ASP A 435 22.839 39.275 1.887 1.00 48.85 C ATOM 1639 O ASP A 435 21.787 39.676 1.373 1.00 53.54 O ATOM 1640 N VAL A 436 23.123 39.414 3.180 1.00 40.69 N ATOM 1641 CA VAL A 436 22.126 39.929 4.110 1.00 46.32 C ATOM 1642 CB VAL A 436 22.425 39.584 5.586 1.00 41.27 C ATOM 1643 CG1 VAL A 436 21.587 40.458 6.485 1.00 46.28 C ATOM 1644 CG2 VAL A 436 22.128 38.126 5.866 1.00 39.91 C ATOM 1645 C VAL A 436 21.984 41.431 3.969 1.00 50.38 C ATOM 1646 O VAL A 436 20.876 41.977 4.029 1.00 49.50 O ATOM 1647 N ASN A 437 23.109 42.102 3.772 1.00 46.09 N ATOM 1648 CA ASN A 437 23.058 43.533 3.585 1.00 45.78 C ATOM 1649 CB ASN A 437 24.462 44.130 3.585 1.00 43.52 C ATOM 1650 CG ASN A 437 25.192 43.898 4.908 1.00 41.74 C ATOM 1651 OD1 ASN A 437 24.573 43.585 5.917 1.00 45.75 O ATOM 1652 ND2 ASN A 437 26.506 44.039 4.898 1.00 42.01 N ATOM 1653 C ASN A 437 22.338 43.749 2.276 1.00 50.16 C ATOM 1654 O ASN A 437 21.483 44.630 2.157 1.00 54.05 O ATOM 1655 N GLY A 438 22.647 42.890 1.314 1.00 43.26 N ATOM 1656 CA GLY A 438 22.002 42.935 0.017 1.00 45.61 C ATOM 1657 C GLY A 438 20.494 42.877 0.131 1.00 48.54 C ATOM 1658 O GLY A 438 19.805 43.777 −0.337 1.00 58.28 O ATOM 1659 N ILE A 439 19.974 41.823 0.754 1.00 50.56 N ATOM 1660 CA ILE A 439 18.513 41.668 0.918 1.00 54.74 C ATOM 1661 CB ILE A 439 18.120 40.285 1.482 1.00 48.10 C ATOM 1662 CG2 ILE A 439 18.209 40.274 3.004 1.00 42.43 C ATOM 1663 CG1 ILE A 439 16.724 39.901 1.004 1.00 42.02 C ATOM 1664 CD1 ILE A 439 16.749 39.086 −0.216 1.00 42.34 C ATOM 1665 C ILE A 439 17.866 42.738 1.801 1.00 50.17 C ATOM 1666 O ILE A 439 16.760 43.185 1.513 1.00 49.03 O ATOM 1667 N ARG A 440 18.547 43.136 2.875 1.00 50.95 N ATOM 1668 CA ARG A 440 18.048 44.194 3.752 1.00 49.73 C ATOM 1669 CB ARG A 440 19.038 44.472 4.902 1.00 51.52 C ATOM 1670 CG ARG A 440 18.525 44.129 6.314 1.00 55.60 C ATOM 1671 CD ARG A 440 19.348 43.061 7.070 1.00 54.50 C ATOM 1672 NE ARG A 440 20.458 43.614 7.857 1.00 62.11 N ATOM 1673 CZ ARG A 440 20.972 43.063 8.967 1.00 58.10 C ATOM 1674 NH1 ARG A 440 20.480 41.930 9.468 1.00 48.42 N ATOM 1675 NH2 ARG A 440 21.989 43.660 9.588 1.00 51.77 N ATOM 1676 C ARG A 440 17.770 45.470 2.943 1.00 49.30 C ATOM 1677 O ARG A 440 16.751 46.130 3.133 1.00 46.23 O ATOM 1678 N HIS A 441 18.663 45.799 2.015 1.00 54.49 N ATOM 1679 CA HIS A 441 18.551 47.053 1.281 1.00 54.42 C ATOM 1680 CB HIS A 441 19.814 47.352 0.477 1.00 56.24 C ATOM 1681 CG HIS A 441 19.583 48.310 −0.647 1.00 62.48 C ATOM 1682 CD2 HIS A 441 19.308 49.636 −0.646 1.00 62.48 C ATOM 1683 ND1 HIS A 441 19.570 47.920 −1.969 1.00 68.84 N ATOM 1684 CE1 HIS A 441 19.322 48.967 −2.736 1.00 68.76 C ATOM 1685 NE2 HIS A 441 19.152 50.021 −1.957 1.00 66.17 N ATOM 1686 C HIS A 441 17.333 47.052 0.366 1.00 61.50 C ATOM 1687 O HIS A 441 16.874 48.103 −0.081 1.00 61.00 O ATOM 1688 N LEU A 442 16.807 45.868 0.082 1.00 61.18 N ATOM 1689 CA LEU A 442 15.534 45.791 −0.614 1.00 60.02 C ATOM 1690 CB LEU A 442 15.490 44.604 −1.593 1.00 57.15 C ATOM 1691 CG LEU A 442 16.549 44.520 −2.703 1.00 62.61 C ATOM 1692 CD1 LEU A 442 17.570 43.429 −2.385 1.00 60.59 C ATOM 1693 CD2 LEU A 442 15.935 44.266 −4.089 1.00 54.09 C ATOM 1694 C LEU A 442 14.361 45.740 0.375 1.00 53.53 C ATOM 1695 O LEU A 442 13.409 46.509 0.257 1.00 65.07 O ATOM 1696 N TYR A 443 14.418 44.857 1.361 1.00 51.44 N ATOM 1697 CA TYR A 443 13.205 44.593 2.135 1.00 54.18 C ATOM 1698 CB TYR A 443 12.864 43.111 2.072 1.00 51.32 C ATOM 1699 CG TYR A 443 12.546 42.682 0.656 1.00 53.72 C ATOM 1700 CD1 TYR A 443 13.546 42.246 −0.205 1.00 49.74 C ATOM 1701 CE1 TYR A 443 13.253 41.863 −1.503 1.00 52.63 C ATOM 1702 CD2 TYR A 443 11.249 42.754 0.167 1.00 58.07 C ATOM 1703 CE2 TYR A 443 10.944 42.376 −1.129 1.00 54.06 C ATOM 1704 CZ TYR A 443 11.945 41.932 −1.962 1.00 55.04 C ATOM 1705 OH TYR A 443 11.624 41.560 −3.254 1.00 46.47 O ATOM 1706 C TYR A 443 13.129 45.157 3.554 1.00 58.93 C ATOM 1707 O TYR A 443 12.354 46.073 3.808 1.00 63.59 O ATOM 1708 N GLY A 444 13.924 44.617 4.470 1.00 69.46 N ATOM 1709 CA GLY A 444 13.893 45.029 5.870 1.00 71.62 C ATOM 1710 C GLY A 444 13.256 46.389 6.115 1.00 76.12 C ATOM 1711 O GLY A 444 13.172 46.871 7.251 1.00 81.53 O ATOM 1712 ZN ZN A 500 23.548 33.554 −9.605 1.00 47.65 Zn ATOM 1713 ZN ZN A 501 15.454 28.916 −18.118 1.00 56.09 Zn ATOM 1714 CA CA A 502 25.015 22.335 −16.543 1.00 57.10 Ca ATOM 1715 CA CA A 503 20.280 13.825 −13.592 1.00 80.84 Ca ATOM 1716 CA CA A 504 5.589 33.639 −11.998 1.00 82.70 Ca TER 1717 CA A 504 ATOM 1718 CB ASP B 41 4.270 13.968 42.643 1.00 83.25 C ATOM 1719 CG ASP B 41 4.825 14.696 43.798 1.00 88.72 C ATOM 1720 OD1 ASP B 41 6.018 14.510 44.020 1.00 87.83 O ATOM 1721 OD2 ASP B 41 4.114 15.457 44.457 1.00 76.09 O ATOM 1722 C ASP B 41 4.907 15.486 40.853 1.00 70.69 C ATOM 1723 O ASP B 41 4.925 15.724 39.660 1.00 70.32 O ATOM 1724 N ASP B 41 6.530 13.834 41.841 1.00 67.79 N ATOM 1725 CA ASP B 41 5.159 14.095 41.428 1.00 73.66 C ATOM 1726 N ARG B 42 4.624 16.604 41.486 1.00 72.48 N ATOM 1727 CA ARG B 42 4.368 18.018 41.604 1.00 66.91 C ATOM 1728 CB ARG B 42 3.125 18.271 42.425 1.00 66.94 C ATOM 1729 CG ARG B 42 2.746 19.692 42.596 1.00 65.17 C ATOM 1730 CD ARG B 42 1.469 19.767 43.362 1.00 66.64 C ATOM 1731 NE ARG B 42 0.970 21.110 43.583 1.00 68.09 N ATOM 1732 CZ ARG B 42 −0.234 21.365 44.068 1.00 68.75 C ATOM 1733 NH1 ARG B 42 −1.011 20.363 44.393 1.00 69.89 N ATOM 1734 NH2 ARG B 42 −0.655 22.603 44.239 1.00 58.10 N ATOM 1735 C ARG B 42 5.593 18.530 42.289 1.00 69.25 C ATOM 1736 O ARG B 42 5.654 19.646 42.712 1.00 63.57 O ATOM 1737 N GLN B 43 6.337 17.655 42.776 1.00 73.86 N ATOM 1738 CA GLN B 43 7.693 18.098 43.056 1.00 74.11 C ATOM 1739 CB GLN B 43 8.548 16.887 43.488 1.00 75.05 C ATOM 1740 CG GLN B 43 7.888 15.506 43.204 1.00 79.14 C ATOM 1741 CD GLN B 43 8.888 14.379 42.888 1.00 82.69 C ATOM 1742 OE1 GLN B 43 8.519 13.323 42.348 1.00 68.25 O ATOM 1743 NE2 GLN B 43 10.155 14.604 43.222 1.00 85.37 N ATOM 1744 C GLN B 43 8.255 18.689 41.763 1.00 67.21 C ATOM 1745 O GLN B 43 8.653 19.852 41.702 1.00 62.35 O ATOM 1746 N LEU B 44 8.259 17.865 40.724 1.00 66.90 N ATOM 1747 CA LEU B 44 8.830 18.229 39.439 1.00 61.56 C ATOM 1748 CB LEU B 44 8.398 17.214 38.381 1.00 60.82 C ATOM 1749 CG LEU B 44 8.962 17.369 36.968 1.00 60.80 C ATOM 1750 CD1 LEU B 44 9.017 16.027 36.251 1.00 66.89 C ATOM 1751 CD2 LEU B 44 8.155 18.363 36.179 1.00 52.17 C ATOM 1752 C LEU B 44 8.450 19.645 39.023 1.00 62.06 C ATOM 1753 O LEU B 44 9.276 20.392 38.498 1.00 62.99 O ATOM 1754 N ALA B 45 7.204 20.017 39.276 1.00 55.23 N ATOM 1755 CA ALA B 45 6.685 21.285 38.797 1.00 56.21 C ATOM 1756 CB ALA B 45 5.150 21.292 38.865 1.00 60.81 C ATOM 1757 C ALA B 45 7.253 22.481 39.544 1.00 54.77 C ATOM 1758 O ALA B 45 7.650 23.471 38.929 1.00 54.65 O ATOM 1759 N GLU B 46 7.261 22.391 40.872 1.00 61.93 N ATOM 1760 CA GLU B 46 7.696 23.487 41.734 1.00 55.24 C ATOM 1761 CB GLU B 46 7.400 23.160 43.201 1.00 58.14 C ATOM 1762 CG GLU B 46 5.936 23.307 43.594 1.00 62.59 C ATOM 1763 CD GLU B 46 5.546 22.425 44.775 1.00 71.15 C ATOM 1764 OE1 GLU B 46 6.399 21.625 45.222 1.00 74.21 O ATOM 1765 OE2 GLU B 46 4.383 22.527 45.248 1.00 68.52 O ATOM 1766 C GLU B 46 9.176 23.748 41.562 1.00 54.94 C ATOM 1767 O GLU B 46 9.633 24.876 41.731 1.00 51.82 O ATOM 1768 N GLU B 47 9.921 22.697 41.232 1.00 53.12 N ATOM 1769 CA GLU B 47 11.359 22.820 41.033 1.00 59.30 C ATOM 1770 CB GLU B 47 12.017 21.438 41.015 1.00 60.13 C ATOM 1771 CG GLU B 47 11.327 20.415 41.906 1.00 67.81 C ATOM 1772 CD GLU B 47 12.047 20.161 43.225 1.00 67.34 C ATOM 1773 OE1 GLU B 47 12.832 19.181 43.298 1.00 61.50 O ATOM 1774 OE2 GLU B 47 11.813 20.928 44.189 1.00 63.79 O ATOM 1775 C GLU B 47 11.633 23.551 39.720 1.00 54.56 C ATOM 1776 O GLU B 47 12.476 24.462 39.640 1.00 45.94 O ATOM 1777 N TYR B 48 10.901 23.145 38.690 1.00 48.82 N ATOM 1778 CA TYR B 48 11.002 23.762 37.389 1.00 44.30 C ATOM 1779 CB TYR B 48 10.026 23.096 36.440 1.00 47.32 C ATOM 1780 CG TYR B 48 10.226 23.495 35.005 1.00 48.59 C ATOM 1781 CD1 TYR B 48 9.803 24.733 34.538 1.00 43.08 C ATOM 1782 CE1 TYR B 48 10.006 25.101 33.215 1.00 46.15 C ATOM 1783 CD2 TYR B 48 10.849 22.629 34.105 1.00 53.64 C ATOM 1784 CE2 TYR B 48 11.038 22.984 32.769 1.00 44.88 C ATOM 1785 CZ TYR B 48 10.620 24.222 32.340 1.00 40.08 C ATOM 1786 OH TYR B 48 10.791 24.564 31.030 1.00 40.71 O ATOM 1787 C TYR B 48 10.669 25.238 37.470 1.00 48.17 C ATOM 1788 O TYR B 48 11.444 26.083 37.027 1.00 46.89 O ATOM 1789 N LEU B 49 9.503 25.541 38.031 1.00 46.26 N ATOM 1790 CA LEU B 49 9.016 26.911 38.098 1.00 47.36 C ATOM 1791 CB LEU B 49 7.646 26.960 38.778 1.00 46.06 C ATOM 1792 CG LEU B 49 6.470 26.402 37.990 1.00 43.84 C ATOM 1793 CD1 LEU B 49 5.267 26.210 38.894 1.00 43.47 C ATOM 1794 CD2 LEU B 49 6.140 27.330 36.833 1.00 44.24 C ATOM 1795 C LEU B 49 9.984 27.802 38.858 1.00 48.64 C ATOM 1796 O LEU B 49 10.182 28.966 38.508 1.00 48.13 O ATOM 1797 N TYR B 50 10.580 27.262 39.910 1.00 45.69 N ATOM 1798 CA TYR B 50 11.397 28.073 40.779 1.00 46.32 C ATOM 1799 CB TYR B 50 11.600 27.396 42.136 1.00 52.89 C ATOM 1800 CG TYR B 50 12.746 28.002 42.887 1.00 54.48 C ATOM 1801 CD1 TYR B 50 12.568 29.162 43.619 1.00 57.66 C ATOM 1802 CE1 TYR B 50 13.612 29.750 44.300 1.00 62.99 C ATOM 1803 CD2 TYR B 50 14.020 27.443 42.827 1.00 56.12 C ATOM 1804 CE2 TYR B 50 15.083 28.024 43.506 1.00 58.75 C ATOM 1805 CZ TYR B 50 14.868 29.183 44.242 1.00 66.04 C ATOM 1806 OH TYR B 50 15.897 29.789 44.931 1.00 78.56 O ATOM 1807 C TYR B 50 12.732 28.301 40.107 1.00 51.65 C ATOM 1808 O TYR B 50 13.260 29.415 40.098 1.00 54.52 O ATOM 1809 N ARG B 51 13.274 27.236 39.534 1.00 47.08 N ATOM 1810 CA ARG B 51 14.536 27.335 38.832 1.00 44.97 C ATOM 1811 CB ARG B 51 14.938 25.976 38.252 1.00 38.91 C ATOM 1812 CG ARG B 51 16.260 26.000 37.517 1.00 43.42 C ATOM 1813 CD ARG B 51 16.567 24.668 36.823 1.00 51.87 C ATOM 1814 NE ARG B 51 17.211 23.707 37.715 1.00 47.88 N ATOM 1815 CZ ARG B 51 18.477 23.812 38.097 1.00 50.79 C ATOM 1816 NH1 ARG B 51 19.197 24.838 37.655 1.00 46.27 N ATOM 1817 NH2 ARG B 51 19.020 22.907 38.911 1.00 46.92 N ATOM 1818 C ARG B 51 14.505 28.418 37.743 1.00 44.89 C ATOM 1819 O ARG B 51 15.386 29.275 37.701 1.00 39.72 O ATOM 1820 N TYR B 52 13.499 28.393 36.869 1.00 41.41 N ATOM 1821 CA TYR B 52 13.527 29.280 35.700 1.00 46.41 C ATOM 1822 CB TYR B 52 13.024 28.570 34.428 1.00 43.16 C ATOM 1823 CG TYR B 52 13.796 27.299 34.159 1.00 42.17 C ATOM 1824 CD1 TYR B 52 13.255 26.071 34.476 1.00 44.16 C ATOM 1825 CE1 TYR B 52 13.964 24.904 34.275 1.00 44.97 C ATOM 1826 CD2 TYR B 52 15.093 27.333 33.644 1.00 44.33 C ATOM 1827 CE2 TYR B 52 15.815 26.160 33.424 1.00 43.97 C ATOM 1828 CZ TYR B 52 15.235 24.943 33.747 1.00 45.65 C ATOM 1829 OH TYR B 52 15.890 23.747 33.543 1.00 42.35 O ATOM 1830 C TYR B 52 12.864 30.639 35.929 1.00 46.67 C ATOM 1831 O TYR B 52 12.796 31.471 35.020 1.00 45.72 O ATOM 1832 N GLY B 53 12.412 30.868 37.158 1.00 47.04 N ATOM 1833 CA GLY B 53 11.966 32.191 37.563 1.00 50.93 C ATOM 1834 C GLY B 53 10.470 32.429 37.737 1.00 51.15 C ATOM 1835 O GLY B 53 10.061 33.549 38.040 1.00 55.14 O ATOM 1836 N TYR B 54 9.648 31.400 37.560 1.00 45.82 N ATOM 1837 CA TYR B 54 8.197 31.606 37.536 1.00 50.84 C ATOM 1838 CB TYR B 54 7.476 30.424 36.867 1.00 46.17 C ATOM 1839 CG TYR B 54 7.907 30.281 35.434 1.00 49.04 C ATOM 1840 CD1 TYR B 54 9.091 29.622 35.111 1.00 44.96 C ATOM 1841 CE1 TYR B 54 9.505 29.521 33.809 1.00 44.46 C ATOM 1842 CD2 TYR B 54 7.170 30.856 34.404 1.00 49.21 C ATOM 1843 CE2 TYR B 54 7.589 30.764 33.095 1.00 44.23 C ATOM 1844 CZ TYR B 54 8.749 30.090 32.809 1.00 39.77 C ATOM 1845 OH TYR B 54 9.163 29.990 31.517 1.00 45.61 O ATOM 1846 C TYR B 54 7.601 31.948 38.907 1.00 54.91 C ATOM 1847 O TYR B 54 6.565 32.621 38.978 1.00 53.64 O ATOM 1848 N THR B 55 8.279 31.495 39.933 1.00 45.28 N ATOM 1849 CA THR B 55 7.952 31.752 41.313 1.00 48.27 C ATOM 1850 CB THR B 55 8.643 30.702 42.150 1.00 51.17 C ATOM 1851 OG1 THR B 55 7.943 29.471 41.996 1.00 57.40 O ATOM 1852 CG2 THR B 55 8.663 31.059 43.547 1.00 41.80 C ATOM 1853 C THR B 55 8.202 33.224 41.761 1.00 54.15 C ATOM 1854 O THR B 55 7.374 33.820 42.397 1.00 54.77 O ATOM 1855 O ALA B 56 7.930 36.420 39.499 1.00 20.00 O ATOM 1856 N ALA B 56 9.209 33.911 41.294 1.00 20.00 N ATOM 1857 CA ALA B 56 9.058 35.336 41.378 1.00 20.00 C ATOM 1858 C ALA B 56 7.833 35.788 40.545 1.00 20.00 C ATOM 1859 CB ALA B 56 10.290 36.015 40.958 1.00 20.00 C ATOM 1860 O ALA B 57 3.377 36.169 42.068 1.00 20.00 O ATOM 1861 N ALA B 57 6.673 35.394 41.043 1.00 20.00 N ATOM 1862 CA ALA B 57 5.344 35.856 40.648 1.00 20.00 C ATOM 1863 C ALA B 57 4.592 36.007 41.993 1.00 20.00 C ATOM 1864 CB ALA B 57 4.689 34.836 39.793 1.00 20.00 C ATOM 1865 O ALA B 58 5.796 38.448 43.683 1.00 20.00 O ATOM 1866 N ALA B 58 5.388 35.913 43.055 1.00 20.00 N ATOM 1867 CA ALA B 58 5.052 36.266 44.405 1.00 20.00 C ATOM 1868 C ALA B 58 5.398 37.735 44.609 1.00 20.00 C ATOM 1869 CB ALA B 58 5.844 35.404 45.357 1.00 20.00 C ATOM 1870 O ALA B 66 −2.608 27.406 43.594 1.00 20.00 O ATOM 1871 N ALA B 66 −3.236 29.115 45.678 1.00 20.00 N ATOM 1872 CA ALA B 66 −2.373 29.544 44.603 1.00 20.00 C ATOM 1873 C ALA B 66 −1.920 28.387 43.703 1.00 20.00 C ATOM 1874 CB ALA B 66 −1.188 30.347 45.181 1.00 20.00 C ATOM 1875 N LEU B 67 −0.772 28.537 43.064 1.00 42.04 N ATOM 1876 CA LEU B 67 −0.196 27.655 42.033 1.00 50.92 C ATOM 1877 CB LEU B 67 −0.050 26.184 42.414 1.00 58.64 C ATOM 1878 CG LEU B 67 1.407 25.790 42.126 1.00 52.48 C ATOM 1879 CD1 LEU B 67 2.269 25.653 43.349 1.00 52.32 C ATOM 1880 CD2 LEU B 67 1.668 24.742 41.150 1.00 54.42 C ATOM 1881 C LEU B 67 −0.630 27.803 40.596 1.00 50.20 C ATOM 1882 O LEU B 67 0.186 27.950 39.746 1.00 51.48 O ATOM 1883 N GLY B 68 −1.905 27.772 40.313 1.00 51.51 N ATOM 1884 CA GLY B 68 −2.343 27.911 38.944 1.00 45.43 C ATOM 1885 C GLY B 68 −1.844 29.096 38.168 1.00 49.61 C ATOM 1886 O GLY B 68 −1.860 29.081 36.972 1.00 52.97 O ATOM 1887 N PRO B 69 −1.426 30.139 38.846 1.00 46.55 N ATOM 1888 CD PRO B 69 −2.344 30.493 39.922 1.00 41.74 C ATOM 1889 CA PRO B 69 −0.968 31.336 38.172 1.00 50.55 C ATOM 1890 CB PRO B 69 −1.186 32.406 39.231 1.00 50.74 C ATOM 1891 CG PRO B 69 −1.834 31.761 40.342 1.00 42.79 C ATOM 1892 C PRO B 69 0.481 31.322 37.737 1.00 49.09 C ATOM 1893 O PRO B 69 0.855 32.092 36.899 1.00 53.14 O ATOM 1894 N ALA B 70 1.283 30.464 38.320 1.00 51.50 N ATOM 1895 CA ALA B 70 2.663 30.349 37.974 1.00 46.90 C ATOM 1896 CB ALA B 70 3.392 29.707 39.087 1.00 48.79 C ATOM 1897 C ALA B 70 2.749 29.499 36.751 1.00 47.70 C ATOM 1898 O ALA B 70 3.560 29.729 35.913 1.00 47.05 O ATOM 1899 N LEU B 71 1.897 28.496 36.670 1.00 39.58 N ATOM 1900 CA LEU B 71 1.761 27.681 35.469 1.00 51.55 C ATOM 1901 CB LEU B 71 0.720 26.584 35.709 1.00 49.02 C ATOM 1902 CG LEU B 71 1.002 25.752 36.960 1.00 51.84 C ATOM 1903 CD1 LEU B 71 −0.212 24.923 37.328 1.00 54.73 C ATOM 1904 CD2 LEU B 71 2.215 24.870 36.750 1.00 50.67 C ATOM 1905 C LEU B 71 1.386 28.516 34.232 1.00 46.05 C ATOM 1906 O LEU B 71 1.909 28.306 33.143 1.00 37.81 O ATOM 1907 N LEU B 72 0.478 29.459 34.424 1.00 44.27 N ATOM 1908 CA LEU B 72 0.014 30.305 33.356 1.00 44.08 C ATOM 1909 CB LEU B 72 −1.115 31.192 33.843 1.00 46.39 C ATOM 1910 CG LEU B 72 −2.411 30.390 33.822 1.00 49.30 C ATOM 1911 CD1 LEU B 72 −3.418 31.009 34.735 1.00 48.38 C ATOM 1912 CD2 LEU B 72 −2.941 30.268 32.390 1.00 50.63 C ATOM 1913 C LEU B 72 1.113 31.139 32.743 1.00 51.67 C ATOM 1914 O LEU B 72 1.151 31.310 31.527 1.00 52.00 O ATOM 1915 N LEU B 73 2.007 31.654 33.581 1.00 52.72 N ATOM 1916 CA LEU B 73 3.142 32.454 33.113 1.00 48.71 C ATOM 1917 CB LEU B 73 3.898 32.972 34.322 1.00 43.97 C ATOM 1918 CG LEU B 73 2.996 33.888 35.119 1.00 53.68 C ATOM 1919 CD1 LEU B 73 3.068 33.562 36.626 1.00 54.42 C ATOM 1920 CD2 LEU B 73 3.357 35.337 34.800 1.00 48.14 C ATOM 1921 C LEU B 73 4.077 31.616 32.246 1.00 50.60 C ATOM 1922 O LEU B 73 4.693 32.094 31.283 1.00 46.57 O ATOM 1923 N LEU B 74 4.175 30.354 32.639 1.00 48.06 N ATOM 1924 CA LEU B 74 4.967 29.358 31.964 1.00 44.38 C ATOM 1925 CB LEU B 74 5.073 28.142 32.881 1.00 43.61 C ATOM 1926 CG LEU B 74 5.523 26.794 32.345 1.00 43.90 C ATOM 1927 CD1 LEU B 74 6.656 26.981 31.376 1.00 50.89 C ATOM 1928 CD2 LEU B 74 5.960 25.976 33.533 1.00 48.19 C ATOM 1929 C LEU B 74 4.300 29.013 30.641 1.00 46.62 C ATOM 1930 O LEU B 74 4.932 29.030 29.594 1.00 49.23 O ATOM 1931 N GLN B 75 3.005 28.739 30.692 1.00 47.87 N ATOM 1932 CA GLN B 75 2.248 28.447 29.492 1.00 45.65 C ATOM 1933 CB GLN B 75 0.797 28.120 29.846 1.00 49.31 C ATOM 1934 CG GLN B 75 0.622 26.713 30.421 1.00 47.10 C ATOM 1935 CD GLN B 75 −0.503 26.624 31.440 1.00 49.82 C ATOM 1936 OE1 GLN B 75 −1.314 27.541 31.576 1.00 49.78 O ATOM 1937 NE2 GLN B 75 −0.555 25.514 32.163 1.00 48.43 N ATOM 1938 C GLN B 75 2.359 29.606 28.512 1.00 47.55 C ATOM 1939 O GLN B 75 2.631 29.390 27.343 1.00 48.73 O ATOM 1940 N LYS B 76 2.194 30.836 28.992 1.00 46.78 N ATOM 1941 CA LYS B 76 2.385 31.999 28.131 1.00 49.72 C ATOM 1942 CB LYS B 76 2.146 33.306 28.896 1.00 47.68 C ATOM 1943 CG LYS B 76 0.885 33.330 29.735 1.00 59.50 C ATOM 1944 CD LYS B 76 −0.252 34.109 29.087 1.00 63.81 C ATOM 1945 CE LYS B 76 −1.331 34.426 30.128 1.00 64.47 C ATOM 1946 NZ LYS B 76 −0.700 34.859 31.426 1.00 58.06 N ATOM 1947 C LYS B 76 3.813 32.007 27.581 1.00 57.61 C ATOM 1948 O LYS B 76 4.032 32.222 26.378 1.00 56.86 O ATOM 1949 N GLN B 77 4.778 31.773 28.472 1.00 51.59 N ATOM 1950 CA GLN B 77 6.196 31.856 28.137 1.00 51.45 C ATOM 1951 CB GLN B 77 7.048 31.678 29.384 1.00 52.37 C ATOM 1952 CG GLN B 77 8.521 31.870 29.125 1.00 50.47 C ATOM 1953 CD GLN B 77 8.887 33.336 29.014 1.00 58.07 C ATOM 1954 OE1 GLN B 77 8.309 34.183 29.706 1.00 55.27 O ATOM 1955 NE2 GLN B 77 9.858 33.648 28.152 1.00 56.93 N ATOM 1956 C GLN B 77 6.634 30.821 27.120 1.00 50.91 C ATOM 1957 O GLN B 77 7.419 31.116 26.226 1.00 49.86 O ATOM 1958 N LEU B 78 6.132 29.603 27.268 1.00 49.35 N ATOM 1959 CA LEU B 78 6.502 28.521 26.371 1.00 49.59 C ATOM 1960 CB LEU B 78 6.524 27.209 27.139 1.00 45.14 C ATOM 1961 CG LEU B 78 7.607 27.155 28.192 1.00 48.66 C ATOM 1962 CD1 LEU B 78 7.851 25.719 28.571 1.00 52.12 C ATOM 1963 CD2 LEU B 78 8.863 27.786 27.619 1.00 51.85 C ATOM 1964 C LEU B 78 5.572 28.381 25.162 1.00 50.72 C ATOM 1965 O LEU B 78 5.739 27.464 24.354 1.00 48.94 O ATOM 1966 N SER B 79 4.600 29.284 25.043 1.00 51.27 N ATOM 1967 CA SER B 79 3.581 29.192 23.993 1.00 52.03 C ATOM 1968 CB SER B 79 4.180 29.447 22.611 1.00 46.44 C ATOM 1969 OG SER B 79 4.538 30.809 22.488 1.00 50.15 O ATOM 1970 C SER B 79 2.866 27.845 24.025 1.00 50.70 C ATOM 1971 O SER B 79 2.884 27.092 23.050 1.00 50.22 O ATOM 1972 N LEU B 80 2.277 27.553 25.178 1.00 49.94 N ATOM 1973 CA LEU B 80 1.455 26.382 25.403 1.00 50.88 C ATOM 1974 CB LEU B 80 2.020 25.579 26.568 1.00 47.88 C ATOM 1975 CG LEU B 80 3.430 25.011 26.591 1.00 53.46 C ATOM 1976 CD1 LEU B 80 3.654 24.342 27.960 1.00 54.07 C ATOM 1977 CD2 LEU B 80 3.660 24.025 25.442 1.00 54.57 C ATOM 1978 C LEU B 80 0.051 26.871 25.790 1.00 55.38 C ATOM 1979 O LEU B 80 −0.100 28.003 26.265 1.00 48.86 O ATOM 1980 N PRO B 81 −0.977 26.016 25.615 1.00 55.87 N ATOM 1981 CD PRO B 81 −0.902 24.595 25.234 1.00 57.85 C ATOM 1982 CA PRO B 81 −2.336 26.401 25.999 1.00 55.92 C ATOM 1983 CB PRO B 81 −3.119 25.089 25.858 1.00 56.90 C ATOM 1984 CG PRO B 81 −2.324 24.243 24.943 1.00 43.55 C ATOM 1985 C PRO B 81 −2.375 26.847 27.460 1.00 52.47 C ATOM 1986 O PRO B 81 −2.129 26.015 28.329 1.00 50.16 O ATOM 1987 N GLU B 82 −2.647 28.128 27.710 1.00 53.49 N ATOM 1988 CA GLU B 82 −2.826 28.647 29.061 1.00 50.62 C ATOM 1989 CB GLU B 82 −2.993 30.172 29.047 1.00 56.07 C ATOM 1990 CG GLU B 82 −1.728 30.963 28.744 1.00 55.60 C ATOM 1991 CD GLU B 82 −1.644 31.361 27.296 1.00 63.99 C ATOM 1992 OE1 GLU B 82 −0.860 32.276 26.959 1.00 62.82 O ATOM 1993 OE2 GLU B 82 −2.381 30.758 26.485 1.00 74.92 O ATOM 1994 C GLU B 82 −4.045 28.011 29.737 1.00 53.29 C ATOM 1995 O GLU B 82 −5.130 28.598 29.781 1.00 51.58 O ATOM 1996 N THR B 83 −3.867 26.804 30.252 1.00 48.74 N ATOM 1997 CA THR B 83 −4.947 26.103 30.900 1.00 42.52 C ATOM 1998 CB THR B 83 −4.840 24.597 30.715 1.00 41.01 C ATOM 1999 OG1 THR B 83 −3.788 24.102 31.543 1.00 45.14 O ATOM 2000 CG2 THR B 83 −4.562 24.236 29.280 1.00 43.07 C ATOM 2001 C THR B 83 −4.837 26.339 32.387 1.00 49.10 C ATOM 2002 O THR B 83 −5.675 25.865 33.154 1.00 48.31 O ATOM 2003 N GLY B 84 −3.786 27.048 32.795 1.00 49.76 N ATOM 2004 CA GLY B 84 −3.467 27.205 34.207 1.00 50.96 C ATOM 2005 C GLY B 84 −3.413 25.890 34.967 1.00 47.75 C ATOM 2006 O GLY B 84 −3.328 25.877 36.189 1.00 58.69 O ATOM 2007 N GLU B 85 −3.435 24.780 34.239 1.00 49.08 N ATOM 2008 CA GLU B 85 −3.564 23.457 34.835 1.00 51.07 C ATOM 2009 CB GLU B 85 −4.746 22.727 34.196 1.00 50.40 C ATOM 2010 CG GLU B 85 −5.505 21.833 35.160 1.00 56.50 C ATOM 2011 CD GLU B 85 −6.104 22.608 36.314 1.00 54.88 C ATOM 2012 OE1 GLU B 85 −5.922 22.170 37.472 1.00 55.52 O ATOM 2013 OE2 GLU B 85 −6.738 23.658 36.062 1.00 53.99 O ATOM 2014 C GLU B 85 −2.293 22.635 34.640 1.00 54.43 C ATOM 2015 O GLU B 85 −1.627 22.735 33.606 1.00 52.41 O ATOM 2016 N LEU B 86 −1.955 21.816 35.632 1.00 55.34 N ATOM 2017 CA LEU B 86 −0.776 20.965 35.527 1.00 48.00 C ATOM 2018 CB LEU B 86 −0.290 20.538 36.908 1.00 47.31 C ATOM 2019 CG LEU B 86 1.065 19.844 36.916 1.00 55.60 C ATOM 2020 CD1 LEU B 86 1.944 20.450 35.862 1.00 46.17 C ATOM 2021 CD2 LEU B 86 1.704 19.951 38.294 1.00 66.48 C ATOM 2022 C LEU B 86 −1.108 19.756 34.661 1.00 49.70 C ATOM 2023 O LEU B 86 −1.050 18.618 35.111 1.00 47.88 O ATOM 2024 N ASP B 87 −1.438 20.030 33.401 1.00 53.60 N ATOM 2025 CA ASP B 87 −1.930 19.032 32.454 1.00 46.03 C ATOM 2026 CB ASP B 87 −2.799 19.747 31.442 1.00 43.25 C ATOM 2027 CG ASP B 87 −2.117 20.984 30.884 1.00 48.52 C ATOM 2028 OD1 ASP B 87 −0.867 21.011 30.871 1.00 48.99 O ATOM 2029 OD2 ASP B 87 −2.818 21.927 30.457 1.00 47.11 O ATOM 2030 C ASP B 87 −0.810 18.286 31.725 1.00 50.42 C ATOM 2031 O ASP B 87 0.373 18.501 31.987 1.00 52.06 O ATOM 2032 N SER B 88 −1.189 17.412 30.798 1.00 48.58 N ATOM 2033 CA SER B 88 −0.212 16.609 30.059 1.00 52.39 C ATOM 2034 CB SER B 88 −0.909 15.626 29.111 1.00 51.95 C ATOM 2035 OG SER B 88 −1.724 14.706 29.809 1.00 57.77 O ATOM 2036 C SER B 88 0.774 17.460 29.257 1.00 53.32 C ATOM 2037 O SER B 88 1.969 17.182 29.243 1.00 60.80 O ATOM 2038 N ALA B 89 0.275 18.481 28.577 1.00 48.03 N ATOM 2039 CA ALA B 89 1.131 19.295 27.730 1.00 45.61 C ATOM 2040 CB ALA B 89 0.287 20.216 26.876 1.00 36.83 C ATOM 2041 C ALA B 89 2.160 20.096 28.551 1.00 52.29 C ATOM 2042 O ALA B 89 3.283 20.328 28.090 1.00 52.62 O ATOM 2043 N THR B 90 1.776 20.506 29.763 1.00 49.75 N ATOM 2044 CA THR B 90 2.633 21.324 30.627 1.00 46.94 C ATOM 2045 CB THR B 90 1.802 22.076 31.705 1.00 53.89 C ATOM 2046 OG1 THR B 90 1.050 23.140 31.088 1.00 53.18 O ATOM 2047 CG2 THR B 90 2.695 22.645 32.803 1.00 46.14 C ATOM 2048 C THR B 90 3.710 20.468 31.287 1.00 53.06 C ATOM 2049 O THR B 90 4.884 20.852 31.367 1.00 49.03 O ATOM 2050 N LEU B 91 3.361 19.279 31.719 1.00 53.98 N ATOM 2051 CA LEU B 91 4.349 18.365 32.267 1.00 54.98 C ATOM 2052 CB LEU B 91 3.643 17.205 32.911 1.00 55.84 C ATOM 2053 CG LEU B 91 3.193 17.406 34.325 1.00 62.72 C ATOM 2054 CD1 LEU B 91 2.079 16.476 34.560 1.00 69.76 C ATOM 2055 CD2 LEU B 91 4.320 17.096 35.201 1.00 58.96 C ATOM 2056 C LEU B 91 5.303 17.834 31.221 1.00 57.62 C ATOM 2057 O LEU B 91 6.425 17.520 31.490 1.00 51.02 O ATOM 2058 N LYS B 92 4.816 17.698 30.015 1.00 56.12 N ATOM 2059 CA LYS B 92 5.666 17.271 28.912 1.00 49.79 C ATOM 2060 CB LYS B 92 4.839 17.103 27.637 1.00 47.78 C ATOM 2061 CG LYS B 92 5.651 16.958 26.381 1.00 46.22 C ATOM 2062 CD LYS B 92 5.383 18.130 25.452 1.00 54.69 C ATOM 2063 CE LYS B 92 6.350 18.149 24.248 1.00 61.93 C ATOM 2064 NZ LYS B 92 6.198 16.986 23.320 1.00 46.05 N ATOM 2065 C LYS B 92 6.775 18.283 28.709 1.00 52.62 C ATOM 2066 O LYS B 92 7.951 17.927 28.694 1.00 54.23 O ATOM 2067 N ALA B 93 6.399 19.553 28.590 1.00 55.23 N ATOM 2068 CA ALA B 93 7.374 20.626 28.415 1.00 47.69 C ATOM 2069 CB ALA B 93 6.678 21.962 28.280 1.00 48.60 C ATOM 2070 C ALA B 93 8.355 20.654 29.580 1.00 50.34 C ATOM 2071 O ALA B 93 9.569 20.700 29.382 1.00 52.21 O ATOM 2072 N MET B 94 7.817 20.614 30.793 1.00 51.09 N ATOM 2073 CA MET B 94 8.637 20.661 31.997 1.00 51.97 C ATOM 2074 CB MET B 94 7.762 20.596 33.237 1.00 49.57 C ATOM 2075 CG MET B 94 6.923 21.833 33.468 1.00 51.26 C ATOM 2076 SD MET B 94 6.156 21.678 35.084 1.00 47.56 S ATOM 2077 CE MET B 94 5.723 23.391 35.442 1.00 40.60 C ATOM 2078 C MET B 94 9.662 19.538 32.054 1.00 53.18 C ATOM 2079 O MET B 94 10.717 19.698 32.658 1.00 49.72 O ATOM 2080 N ARG B 95 9.356 18.410 31.417 1.00 56.06 N ATOM 2081 CA ARG B 95 10.259 17.258 31.422 1.00 50.30 C ATOM 2082 CB ARG B 95 9.470 15.950 31.469 1.00 56.50 C ATOM 2083 CG ARG B 95 9.273 15.394 32.870 1.00 62.34 C ATOM 2084 CD ARG B 95 8.979 13.902 32.824 1.00 62.36 C ATOM 2085 NE ARG B 95 7.557 13.609 32.989 1.00 72.70 N ATOM 2086 CZ ARG B 95 6.992 13.273 34.145 1.00 72.52 C ATOM 2087 NH1 ARG B 95 7.720 13.184 35.251 1.00 68.51 N ATOM 2088 NH2 ARG B 95 5.696 13.019 34.189 1.00 75.03 N ATOM 2089 C ARG B 95 11.207 17.209 30.231 1.00 51.21 C ATOM 2090 O ARG B 95 12.065 16.334 30.172 1.00 48.41 O ATOM 2091 N THR B 96 11.049 18.115 29.268 1.00 47.61 N ATOM 2092 CA THR B 96 11.957 18.096 28.129 1.00 51.48 C ATOM 2093 CB THR B 96 11.266 18.478 26.794 1.00 47.32 C ATOM 2094 OG1 THR B 96 12.101 19.379 26.059 1.00 48.87 O ATOM 2095 CG2 THR B 96 9.959 19.140 27.045 1.00 48.06 C ATOM 2096 C THR B 96 13.201 18.951 28.391 1.00 49.48 C ATOM 2097 O THR B 96 13.094 20.032 28.979 1.00 42.82 O ATOM 2098 N PRO B 97 14.378 18.455 27.950 1.00 46.85 N ATOM 2099 CD PRO B 97 14.467 17.278 27.071 1.00 46.16 C ATOM 2100 CA PRO B 97 15.698 19.056 28.175 1.00 43.98 C ATOM 2101 CB PRO B 97 16.660 18.109 27.448 1.00 44.20 C ATOM 2102 CG PRO B 97 15.899 16.857 27.224 1.00 47.91 C ATOM 2103 C PRO B 97 15.758 20.414 27.532 1.00 44.23 C ATOM 2104 O PRO B 97 15.194 20.625 26.461 1.00 43.63 O ATOM 2105 N ARG B 98 16.451 21.328 28.192 1.00 47.24 N ATOM 2106 CA ARG B 98 16.443 22.717 27.792 1.00 47.91 C ATOM 2107 CB ARG B 98 15.295 23.433 28.480 1.00 40.48 C ATOM 2108 CG ARG B 98 15.423 23.430 29.999 1.00 44.00 C ATOM 2109 CD ARG B 98 14.477 24.439 30.636 1.00 42.89 C ATOM 2110 NE ARG B 98 15.016 25.796 30.570 1.00 40.97 N ATOM 2111 CZ ARG B 98 14.272 26.895 30.496 1.00 40.29 C ATOM 2112 NH1 ARG B 98 12.949 26.810 30.450 1.00 36.03 N ATOM 2113 NH2 ARG B 98 14.854 28.080 30.445 1.00 41.17 N ATOM 2114 C ARG B 98 17.735 23.410 28.182 1.00 44.27 C ATOM 2115 O ARG B 98 18.654 22.794 28.726 1.00 44.27 O ATOM 2116 N CYS B 99 17.781 24.704 27.885 1.00 41.10 N ATOM 2117 CA CYS B 99 18.846 25.575 28.335 1.00 39.98 C ATOM 2118 CB CYS B 99 18.827 26.869 27.540 1.00 42.96 C ATOM 2119 SG CYS B 99 19.942 28.076 28.253 1.00 46.56 S ATOM 2120 C CYS B 99 18.678 25.920 29.811 1.00 44.32 C ATOM 2121 O CYS B 99 17.564 26.000 30.312 1.00 41.65 O ATOM 2122 N GLY B 100 19.797 26.145 30.491 1.00 45.28 N ATOM 2123 CA GLY B 100 19.794 26.518 31.887 1.00 39.07 C ATOM 2124 C GLY B 100 19.355 27.946 32.133 1.00 43.31 C ATOM 2125 O GLY B 100 18.754 28.248 33.164 1.00 50.02 O ATOM 2126 N VAL B 101 19.644 28.843 31.204 1.00 40.78 N ATOM 2127 CA VAL B 101 19.275 30.227 31.436 1.00 44.42 C ATOM 2128 CB VAL B 101 19.655 31.119 30.261 1.00 43.99 C ATOM 2129 CG1 VAL B 101 19.245 32.570 30.556 1.00 47.54 C ATOM 2130 CG2 VAL B 101 21.148 31.033 30.010 1.00 43.85 C ATOM 2131 C VAL B 101 17.779 30.385 31.786 1.00 47.40 C ATOM 2132 O VAL B 101 16.918 29.884 31.058 1.00 45.60 O ATOM 2133 N PRO B 102 17.477 31.061 32.919 1.00 43.88 N ATOM 2134 CD PRO B 102 18.509 31.419 33.908 1.00 44.31 C ATOM 2135 CA PRO B 102 16.128 31.448 33.375 1.00 48.59 C ATOM 2136 CB PRO B 102 16.421 32.416 34.530 1.00 45.73 C ATOM 2137 CG PRO B 102 17.719 31.967 35.075 1.00 42.92 C ATOM 2138 C PRO B 102 15.289 32.174 32.306 1.00 51.27 C ATOM 2139 O PRO B 102 15.873 32.816 31.426 1.00 51.78 O ATOM 2140 N ASP B 103 13.956 32.087 32.396 1.00 52.15 N ATOM 2141 CA ASP B 103 13.042 32.752 31.449 1.00 48.21 C ATOM 2142 CB ASP B 103 11.892 31.815 31.058 1.00 45.24 C ATOM 2143 CG ASP B 103 12.359 30.421 30.748 1.00 44.34 C ATOM 2144 OD1 ASP B 103 13.469 30.274 30.198 1.00 46.82 O ATOM 2145 OD2 ASP B 103 11.612 29.473 31.037 1.00 38.32 O ATOM 2146 C ASP B 103 12.435 34.061 31.981 1.00 45.02 C ATOM 2147 O ASP B 103 12.082 34.938 31.208 1.00 45.25 O ATOM 2148 N LEU B 104 12.261 34.161 33.296 1.00 50.42 N ATOM 2149 CA LEU B 104 11.806 35.399 33.926 1.00 49.12 C ATOM 2150 CB LEU B 104 10.384 35.255 34.468 1.00 48.54 C ATOM 2151 CG LEU B 104 9.277 34.781 33.525 1.00 50.78 C ATOM 2152 CD1 LEU B 104 7.999 34.511 34.319 1.00 57.37 C ATOM 2153 CD2 LEU B 104 9.009 35.790 32.423 1.00 53.26 C ATOM 2154 C LEU B 104 12.749 35.798 35.067 1.00 59.64 C ATOM 2155 O LEU B 104 13.551 34.981 35.546 1.00 56.14 O ATOM 2156 N GLY B 105 12.616 37.020 35.519 1.00 60.65 N ATOM 2157 CA GLY B 105 13.252 37.429 36.736 1.00 56.94 C ATOM 2158 C GLY B 105 14.666 37.886 36.576 1.00 65.63 C ATOM 2159 O GLY B 105 15.353 37.483 35.666 1.00 64.02 O ATOM 2160 N ARG B 106 15.074 38.742 37.498 1.00 64.07 N ATOM 2161 CA ARG B 106 16.433 39.156 37.640 1.00 72.26 C ATOM 2162 CB ARG B 106 16.541 40.668 37.678 1.00 76.42 C ATOM 2163 CG ARG B 106 16.794 41.317 36.331 1.00 65.95 C ATOM 2164 CD ARG B 106 17.360 40.345 35.303 1.00 68.91 C ATOM 2165 NE ARG B 106 17.183 40.824 33.932 1.00 71.94 N ATOM 2166 CZ ARG B 106 17.853 41.837 33.387 1.00 63.90 C ATOM 2167 NH1 ARG B 106 17.623 42.201 32.141 1.00 57.67 N ATOM 2168 NH2 ARG B 106 18.751 42.488 34.095 1.00 65.93 N ATOM 2169 C ARG B 106 16.882 38.590 38.949 1.00 73.21 C ATOM 2170 O ARG B 106 17.078 39.286 39.879 1.00 76.40 O ATOM 2171 N PHE B 107 17.040 37.296 39.026 1.00 71.68 N ATOM 2172 CA PHE B 107 17.601 36.761 40.205 1.00 75.30 C ATOM 2173 CB PHE B 107 17.712 35.271 40.107 1.00 79.20 C ATOM 2174 CG PHE B 107 16.406 34.595 40.270 1.00 87.63 C ATOM 2175 CD1 PHE B 107 16.023 34.095 41.492 1.00 89.90 C ATOM 2176 CD2 PHE B 107 15.533 34.509 39.220 1.00 84.20 C ATOM 2177 CE1 PHE B 107 14.811 33.497 41.646 1.00 85.03 C ATOM 2178 CE2 PHE B 107 14.335 33.919 39.385 1.00 71.70 C ATOM 2179 CZ PHE B 107 13.975 33.411 40.603 1.00 71.75 C ATOM 2180 C PHE B 107 18.922 37.394 40.334 1.00 70.91 C ATOM 2181 O PHE B 107 19.163 38.091 41.291 1.00 65.04 O ATOM 2182 N GLN B 108 19.790 37.205 39.363 1.00 70.72 N ATOM 2183 CA GLN B 108 21.087 37.834 39.468 1.00 67.59 C ATOM 2184 CB GLN B 108 22.190 36.976 38.957 1.00 57.57 C ATOM 2185 CG GLN B 108 23.455 37.672 39.141 1.00 57.57 C ATOM 2186 CD GLN B 108 24.595 36.778 38.968 1.00 68.33 C ATOM 2187 OE1 GLN B 108 25.731 37.200 39.035 1.00 61.07 O ATOM 2188 NE2 GLN B 108 24.313 35.523 38.717 1.00 57.45 N ATOM 2189 C GLN B 108 21.238 39.181 38.826 1.00 67.96 C ATOM 2190 O GLN B 108 20.581 39.525 37.873 1.00 67.24 O ATOM 2191 N THR B 109 22.158 39.936 39.366 1.00 60.34 N ATOM 2192 CA THR B 109 22.378 41.300 38.900 1.00 64.84 C ATOM 2193 CB THR B 109 22.268 42.324 40.076 1.00 72.36 C ATOM 2194 OG1 THR B 109 21.541 43.486 39.653 1.00 76.39 O ATOM 2195 CG2 THR B 109 23.650 42.732 40.614 1.00 67.41 C ATOM 2196 C THR B 109 23.740 41.401 38.181 1.00 69.53 C ATOM 2197 O THR B 109 24.797 41.063 38.737 1.00 64.83 O ATOM 2198 N PHE B 110 23.706 41.853 36.933 1.00 58.71 N ATOM 2199 CA PHE B 110 24.897 41.865 36.104 1.00 57.37 C ATOM 2200 CB PHE B 110 24.610 41.172 34.764 1.00 54.27 C ATOM 2201 CG PHE B 110 24.374 39.687 34.883 1.00 52.46 C ATOM 2202 CD1 PHE B 110 23.095 39.185 35.073 1.00 58.35 C ATOM 2203 CD2 PHE B 110 25.433 38.793 34.795 1.00 48.15 C ATOM 2204 CE1 PHE B 110 22.877 37.807 35.180 1.00 59.78 C ATOM 2205 CE2 PHE B 110 25.224 37.420 34.900 1.00 50.73 C ATOM 2206 CZ PHE B 110 23.945 36.923 35.096 1.00 50.94 C ATOM 2207 C PHE B 110 25.424 43.286 35.888 1.00 57.96 C ATOM 2208 O PHE B 110 24.781 44.272 36.274 1.00 57.41 O ATOM 2209 N GLU B 111 26.606 43.382 35.287 1.00 53.58 N ATOM 2210 CA GLU B 111 27.199 44.672 34.937 1.00 58.58 C ATOM 2211 CB GLU B 111 28.713 44.633 35.144 1.00 64.39 C ATOM 2212 CG GLU B 111 29.169 44.670 36.583 1.00 69.04 C ATOM 2213 CD GLU B 111 30.638 45.040 36.698 1.00 83.84 C ATOM 2214 OE1 GLU B 111 31.147 45.705 35.765 1.00 78.89 O ATOM 2215 OE2 GLU B 111 31.280 44.671 37.712 1.00 102.30 O ATOM 2216 C GLU B 111 26.918 45.105 33.489 1.00 58.27 C ATOM 2217 O GLU B 111 27.021 44.298 32.552 1.00 58.98 O ATOM 2218 N GLY B 112 26.589 46.384 33.311 1.00 48.61 N ATOM 2219 CA GLY B 112 26.435 46.964 31.989 1.00 47.65 C ATOM 2220 C GLY B 112 25.051 46.770 31.387 1.00 49.32 C ATOM 2221 O GLY B 112 24.196 46.125 31.981 1.00 47.60 O ATOM 2222 N ASP B 113 24.837 47.330 30.199 1.00 49.94 N ATOM 2223 CA ASP B 113 23.565 47.209 29.489 1.00 49.91 C ATOM 2224 CB ASP B 113 23.419 48.327 28.457 1.00 51.80 C ATOM 2225 CG ASP B 113 24.621 48.416 27.527 1.00 54.63 C ATOM 2226 OD1 ASP B 113 25.702 47.935 27.931 1.00 56.67 O ATOM 2227 OD2 ASP B 113 24.498 48.965 26.411 1.00 50.07 O ATOM 2228 C ASP B 113 23.432 45.876 28.768 1.00 49.47 C ATOM 2229 O ASP B 113 22.656 45.771 27.823 1.00 51.04 O ATOM 2230 N LEU B 114 24.208 44.880 29.199 1.00 50.60 N ATOM 2231 CA LEU B 114 24.105 43.507 28.697 1.00 48.83 C ATOM 2232 CB LEU B 114 22.786 42.879 29.139 1.00 45.04 C ATOM 2233 CG LEU B 114 22.476 42.831 30.639 1.00 48.40 C ATOM 2234 CD1 LEU B 114 21.217 42.009 30.882 1.00 41.98 C ATOM 2235 CD2 LEU B 114 23.640 42.262 31.439 1.00 48.44 C ATOM 2236 C LEU B 114 24.246 43.397 27.180 1.00 52.83 C ATOM 2237 O LEU B 114 23.557 42.597 26.540 1.00 55.57 O ATOM 2238 N LYS B 115 25.153 44.189 26.617 1.00 53.08 N ATOM 2239 CA LYS B 115 25.312 44.307 25.176 1.00 50.45 C ATOM 2240 CB LYS B 115 24.413 45.436 24.678 1.00 55.68 C ATOM 2241 CG LYS B 115 24.418 45.651 23.183 1.00 56.29 C ATOM 2242 CD LYS B 115 23.475 46.780 22.794 1.00 59.92 C ATOM 2243 CE LYS B 115 24.233 48.072 22.546 1.00 63.82 C ATOM 2244 NZ LYS B 115 23.318 49.122 22.009 1.00 71.06 N ATOM 2245 C LYS B 115 26.768 44.631 24.858 1.00 51.76 C ATOM 2246 O LYS B 115 27.409 45.381 25.598 1.00 50.92 O ATOM 2247 N TRP B 116 27.303 44.065 23.778 1.00 48.24 N ATOM 2248 CA TRP B 116 28.677 44.378 23.394 1.00 47.21 C ATOM 2249 CB TRP B 116 29.253 43.363 22.396 1.00 48.87 C ATOM 2250 CG TRP B 116 29.385 41.983 22.971 1.00 47.35 C ATOM 2251 CD2 TRP B 116 30.165 41.597 24.115 1.00 45.81 C ATOM 2252 CE2 TRP B 116 29.978 40.217 24.302 1.00 44.11 C ATOM 2253 CE3 TRP B 116 31.010 42.290 24.995 1.00 51.76 C ATOM 2254 CD1 TRP B 116 28.769 40.847 22.531 1.00 45.26 C ATOM 2255 NE1 TRP B 116 29.118 39.781 23.327 1.00 48.12 N ATOM 2256 CZ2 TRP B 116 30.606 39.512 25.324 1.00 41.15 C ATOM 2257 CZ3 TRP B 116 31.630 41.586 26.019 1.00 40.46 C ATOM 2258 CH2 TRP B 116 31.426 40.214 26.169 1.00 43.92 C ATOM 2259 C TRP B 116 28.788 45.794 22.853 1.00 50.49 C ATOM 2260 O TRP B 116 27.826 46.341 22.319 1.00 59.00 O ATOM 2261 N HIS B 117 29.962 46.393 23.003 1.00 55.60 N ATOM 2262 CA HIS B 117 30.180 47.746 22.513 1.00 52.47 C ATOM 2263 CB HIS B 117 30.273 48.740 23.680 1.00 47.92 C ATOM 2264 CG HIS B 117 28.950 49.104 24.288 1.00 58.43 C ATOM 2265 CD2 HIS B 117 28.112 50.143 24.047 1.00 63.59 C ATOM 2266 ND1 HIS B 117 28.361 48.368 25.301 1.00 59.86 N ATOM 2267 CE1 HIS B 117 27.213 48.930 25.645 1.00 56.04 C ATOM 2268 NE2 HIS B 117 27.039 50.010 24.901 1.00 63.81 N ATOM 2269 C HIS B 117 31.436 47.805 21.641 1.00 53.33 C ATOM 2270 O HIS B 117 32.079 48.850 21.542 1.00 53.58 O ATOM 2271 N HIS B 118 31.787 46.683 21.015 1.00 56.76 N ATOM 2272 CA HIS B 118 32.915 46.642 20.068 1.00 57.51 C ATOM 2273 CB HIS B 118 34.257 46.506 20.793 1.00 49.63 C ATOM 2274 CG HIS B 118 34.383 45.259 21.613 1.00 52.76 C ATOM 2275 CD2 HIS B 118 35.196 44.182 21.482 1.00 50.89 C ATOM 2276 ND1 HIS B 118 33.622 45.029 22.737 1.00 52.44 N ATOM 2277 CE1 HIS B 118 33.958 43.861 23.260 1.00 59.24 C ATOM 2278 NE2 HIS B 118 34.912 43.327 22.517 1.00 48.83 N ATOM 2279 C HIS B 118 32.717 45.521 19.045 1.00 58.44 C ATOM 2280 O HIS B 118 32.095 44.505 19.356 1.00 59.48 O ATOM 2281 N HIS B 119 33.241 45.701 17.832 1.00 54.94 N ATOM 2282 CA HIS B 119 32.838 44.841 16.708 1.00 58.12 C ATOM 2283 CB HIS B 119 32.868 45.589 15.362 1.00 64.74 C ATOM 2284 CG HIS B 119 31.659 46.438 15.116 1.00 69.89 C ATOM 2285 CD2 HIS B 119 30.337 46.141 15.172 1.00 64.51 C ATOM 2286 ND1 HIS B 119 31.735 47.778 14.801 1.00 79.66 N ATOM 2287 CE1 HIS B 119 30.515 48.268 14.660 1.00 74.17 C ATOM 2288 NE2 HIS B 119 29.649 47.294 14.880 1.00 69.12 N ATOM 2289 C HIS B 119 33.534 43.487 16.577 1.00 56.14 C ATOM 2290 O HIS B 119 32.932 42.544 16.056 1.00 57.74 O ATOM 2291 N ASN B 120 34.787 43.371 17.014 1.00 55.52 N ATOM 2292 CA ASN B 120 35.449 42.063 16.927 1.00 56.15 C ATOM 2293 CB ASN B 120 36.857 42.116 16.333 1.00 55.69 C ATOM 2294 CG ASN B 120 37.506 40.721 16.268 1.00 62.63 C ATOM 2295 OD1 ASN B 120 36.809 39.698 16.150 1.00 54.59 O ATOM 2296 ND2 ASN B 120 38.839 40.677 16.358 1.00 62.85 N ATOM 2297 C ASN B 120 35.481 41.274 18.219 1.00 53.49 C ATOM 2298 O ASN B 120 36.444 41.345 18.992 1.00 44.51 O ATOM 2299 N ILE B 121 34.416 40.503 18.409 1.00 54.81 N ATOM 2300 CA ILE B 121 34.255 39.629 19.550 1.00 44.74 C ATOM 2301 CB ILE B 121 32.795 39.274 19.722 1.00 43.20 C ATOM 2302 CG2 ILE B 121 32.636 38.132 20.731 1.00 48.08 C ATOM 2303 CG1 ILE B 121 32.030 40.521 20.181 1.00 44.23 C ATOM 2304 CD1 ILE B 121 31.359 41.284 19.088 1.00 42.66 C ATOM 2305 C ILE B 121 35.123 38.373 19.410 1.00 50.08 C ATOM 2306 O ILE B 121 35.116 37.692 18.380 1.00 47.10 O ATOM 2307 N THR B 122 35.889 38.093 20.457 1.00 50.32 N ATOM 2308 CA THR B 122 36.860 37.016 20.435 1.00 44.97 C ATOM 2309 CB THR B 122 38.241 37.521 20.915 1.00 45.93 C ATOM 2310 OG1 THR B 122 38.117 38.151 22.198 1.00 50.15 O ATOM 2311 CG2 THR B 122 38.815 38.534 19.928 1.00 50.31 C ATOM 2312 C THR B 122 36.393 35.891 21.350 1.00 43.95 C ATOM 2313 O THR B 122 35.836 36.154 22.413 1.00 48.37 O ATOM 2314 N TYR B 123 36.602 34.643 20.948 1.00 39.95 N ATOM 2315 CA TYR B 123 36.327 33.543 21.859 1.00 44.47 C ATOM 2316 CB TYR B 123 35.088 32.770 21.441 1.00 45.41 C ATOM 2317 CG TYR B 123 35.186 32.084 20.112 1.00 41.45 C ATOM 2318 CD1 TYR B 123 34.887 32.770 18.951 1.00 40.60 C ATOM 2319 CE1 TYR B 123 34.949 32.156 17.717 1.00 46.20 C ATOM 2320 CD2 TYR B 123 35.534 30.740 20.015 1.00 41.71 C ATOM 2321 CE2 TYR B 123 35.598 30.107 18.771 1.00 44.35 C ATOM 2322 CZ TYR B 123 35.302 30.834 17.629 1.00 42.99 C ATOM 2323 OH TYR B 123 35.346 30.269 16.387 1.00 44.70 O ATOM 2324 C TYR B 123 37.496 32.591 22.055 1.00 47.17 C ATOM 2325 O TYR B 123 38.448 32.582 21.272 1.00 46.04 O ATOM 2326 N TRP B 124 37.411 31.784 23.106 1.00 44.83 N ATOM 2327 CA TRP B 124 38.516 30.910 23.482 1.00 43.67 C ATOM 2328 CB TRP B 124 39.288 31.550 24.629 1.00 42.57 C ATOM 2329 CG TRP B 124 40.384 30.691 25.172 1.00 48.16 C ATOM 2330 CD2 TRP B 124 40.673 30.425 26.556 1.00 47.91 C ATOM 2331 CE2 TRP B 124 41.805 29.584 26.595 1.00 43.35 C ATOM 2332 CE3 TRP B 124 40.077 30.822 27.757 1.00 38.08 C ATOM 2333 CD1 TRP B 124 41.332 30.014 24.451 1.00 42.71 C ATOM 2334 NE1 TRP B 124 42.177 29.337 25.300 1.00 43.45 N ATOM 2335 CZ2 TRP B 124 42.353 29.121 27.782 1.00 41.16 C ATOM 2336 CZ3 TRP B 124 40.625 30.364 28.941 1.00 46.98 C ATOM 2337 CH2 TRP B 124 41.746 29.520 28.948 1.00 51.92 C ATOM 2338 C TRP B 124 38.022 29.538 23.910 1.00 45.39 C ATOM 2339 O TRP B 124 37.501 29.375 25.028 1.00 46.79 O ATOM 2340 N ILE B 125 38.163 28.544 23.038 1.00 39.45 N ATOM 2341 CA ILE B 125 37.711 27.216 23.425 1.00 47.85 C ATOM 2342 CB ILE B 125 37.801 26.158 22.306 1.00 46.33 C ATOM 2343 CG2 ILE B 125 37.741 24.769 22.938 1.00 42.99 C ATOM 2344 CG1 ILE B 125 36.615 26.242 21.334 1.00 50.58 C ATOM 2345 CD1 ILE B 125 36.370 27.596 20.682 1.00 50.31 C ATOM 2346 C ILE B 125 38.624 26.792 24.548 1.00 46.90 C ATOM 2347 O ILE B 125 39.748 26.357 24.301 1.00 49.91 O ATOM 2348 N GLN B 126 38.172 26.927 25.787 1.00 43.94 N ATOM 2349 CA GLN B 126 39.073 26.654 26.893 1.00 43.84 C ATOM 2350 CB GLN B 126 38.649 27.416 28.147 1.00 46.15 C ATOM 2351 CG GLN B 126 39.480 27.087 29.365 1.00 43.96 C ATOM 2352 CD GLN B 126 38.840 27.573 30.655 1.00 51.22 C ATOM 2353 OE1 GLN B 126 37.670 27.978 30.676 1.00 51.22 O ATOM 2354 NE2 GLN B 126 39.607 27.537 31.740 1.00 41.09 N ATOM 2355 C GLN B 126 39.259 25.162 27.186 1.00 44.44 C ATOM 2356 O GLN B 126 40.190 24.779 27.894 1.00 49.63 O ATOM 2357 N ASN B 127 38.385 24.314 26.663 1.00 37.34 N ATOM 2358 CA ASN B 127 38.598 22.871 26.791 0.00 43.20 C ATOM 2359 CB ASN B 127 38.532 22.418 28.253 1.00 34.70 C ATOM 2360 CG ASN B 127 37.124 22.468 28.812 1.00 46.20 C ATOM 2361 OD1 ASN B 127 36.300 23.262 28.365 1.00 45.53 O ATOM 2362 ND2 ASN B 127 36.837 21.612 29.790 0.96 43.78 N ATOM 2363 C ASN B 127 37.644 22.046 25.944 1.00 44.11 C ATOM 2364 O ASN B 127 36.782 22.580 25.255 1.00 45.78 O ATOM 2365 N TYR B 128 37.797 20.732 25.997 1.00 45.10 N ATOM 2366 CA TYR B 128 37.048 19.880 25.095 1.00 47.36 C ATOM 2367 CB TYR B 128 37.978 19.324 24.012 1.00 51.19 C ATOM 2368 CG TYR B 128 38.523 20.400 23.106 1.00 46.90 C ATOM 2369 CD1 TYR B 128 37.912 20.681 21.899 1.00 49.16 C ATOM 2370 CE1 TYR B 128 38.384 21.671 21.069 1.00 54.48 C ATOM 2371 CD2 TYR B 128 39.620 21.161 23.478 1.00 48.89 C ATOM 2372 CE2 TYR B 128 40.111 22.161 22.645 1.00 48.28 C ATOM 2373 CZ TYR B 128 39.481 22.410 21.444 1.00 51.79 C ATOM 2374 OH TYR B 128 39.935 23.392 20.604 1.00 49.69 O ATOM 2375 C TYR B 128 36.333 18.757 25.820 1.00 52.51 C ATOM 2376 O TYR B 128 36.806 18.258 26.841 1.00 53.09 O ATOM 2377 N SER B 129 35.163 18.400 25.304 1.00 51.10 N ATOM 2378 CA SER B 129 34.520 17.160 25.685 1.00 51.43 C ATOM 2379 CB SER B 129 33.008 17.224 25.436 1.00 49.79 C ATOM 2380 OG SER B 129 32.468 15.951 25.101 1.00 43.12 O ATOM 2381 C SER B 129 35.164 16.151 24.771 1.00 46.57 C ATOM 2382 O SER B 129 35.695 16.532 23.741 1.00 50.11 O ATOM 2383 N GLU B 130 35.114 14.874 25.147 1.00 53.25 N ATOM 2384 CA GLU B 130 35.689 13.795 24.343 1.00 55.46 C ATOM 2385 CB GLU B 130 36.219 12.696 25.261 1.00 56.42 C ATOM 2386 CG GLU B 130 37.285 13.152 26.241 1.00 63.08 C ATOM 2387 CD GLU B 130 38.669 13.228 25.616 1.00 67.90 C ATOM 2388 OE1 GLU B 130 39.607 12.599 26.164 1.00 65.20 O ATOM 2389 OE2 GLU B 130 38.816 13.911 24.576 1.00 70.06 O ATOM 2390 C GLU B 130 34.716 13.178 23.311 1.00 54.41 C ATOM 2391 O GLU B 130 35.123 12.389 22.453 1.00 54.32 O ATOM 2392 N ASP B 131 33.439 13.533 23.388 1.00 48.60 N ATOM 2393 CA ASP B 131 32.438 12.883 22.556 1.00 48.15 C ATOM 2394 CB ASP B 131 31.037 13.305 22.998 1.00 50.07 C ATOM 2395 CG ASP B 131 30.845 13.205 24.498 1.00 53.01 C ATOM 2396 OD1 ASP B 131 31.627 12.477 25.144 1.00 58.57 O ATOM 2397 OD2 ASP B 131 29.910 13.848 25.034 1.00 53.80 O ATOM 2398 C ASP B 131 32.643 13.170 21.059 1.00 55.06 C ATOM 2399 O ASP B 131 32.058 12.503 20.193 1.00 50.86 O ATOM 2400 N LEU B 132 33.469 14.169 20.757 1.00 51.43 N ATOM 2401 CA LEU B 132 33.677 14.590 19.377 1.00 47.27 C ATOM 2402 CB LEU B 132 32.676 15.693 18.992 1.00 49.16 C ATOM 2403 CG LEU B 132 31.170 15.386 19.048 1.00 46.90 C ATOM 2404 CD1 LEU B 132 30.335 16.658 18.986 1.00 40.32 C ATOM 2405 CD2 LEU B 132 30.763 14.434 17.940 1.00 39.45 C ATOM 2406 C LEU B 132 35.105 15.081 19.146 1.00 48.95 C ATOM 2407 O LEU B 132 35.708 15.710 20.015 1.00 49.32 O ATOM 2408 N PRO B 133 35.647 14.803 17.957 1.00 48.74 N ATOM 2409 CD PRO B 133 34.979 14.137 16.828 1.00 45.76 C ATOM 2410 CA PRO B 133 36.993 15.256 17.615 1.00 49.75 C ATOM 2411 CB PRO B 133 37.144 14.832 16.155 1.00 49.94 C ATOM 2412 CG PRO B 133 36.111 13.763 15.953 1.00 47.50 C ATOM 2413 C PRO B 133 37.087 16.766 17.723 1.00 49.32 C ATOM 2414 O PRO B 133 36.204 17.473 17.245 1.00 52.24 O ATOM 2415 N ARG B 134 38.154 17.238 18.352 1.00 47.71 N ATOM 2416 CA ARG B 134 38.411 18.650 18.563 1.00 49.45 C ATOM 2417 CB ARG B 134 39.869 18.840 18.986 1.00 53.99 C ATOM 2418 CG ARG B 134 40.255 18.119 20.264 1.00 54.34 C ATOM 2419 CD ARG B 134 41.625 18.588 20.753 1.00 50.57 C ATOM 2420 NE ARG B 134 41.770 18.375 22.182 1.00 51.99 N ATOM 2421 CZ ARG B 134 42.404 19.207 22.998 1.00 55.19 C ATOM 2422 NH1 ARG B 134 42.955 20.313 22.512 1.00 55.84 N ATOM 2423 NH2 ARG B 134 42.486 18.935 24.295 1.00 44.15 N ATOM 2424 C ARG B 134 38.163 19.487 17.322 1.00 48.83 C ATOM 2425 O ARG B 134 37.600 20.575 17.403 1.00 49.69 O ATOM 2426 N ALA B 135 38.634 19.003 16.182 1.00 48.31 N ATOM 2427 CA ALA B 135 38.412 19.702 14.935 1.00 48.68 C ATOM 2428 CB ALA B 135 39.044 18.939 13.792 1.00 42.64 C ATOM 2429 C ALA B 135 36.900 19.878 14.715 1.00 50.13 C ATOM 2430 O ALA B 135 36.433 20.961 14.356 1.00 44.39 O ATOM 2431 N VAL B 136 36.146 18.807 14.949 1.00 43.69 N ATOM 2432 CA VAL B 136 34.695 18.834 14.782 1.00 46.53 C ATOM 2433 CB VAL B 136 34.112 17.449 15.044 1.00 47.28 C ATOM 2434 CG1 VAL B 136 32.628 17.530 15.305 1.00 38.87 C ATOM 2435 CG2 VAL B 136 34.443 16.527 13.887 1.00 43.43 C ATOM 2436 C VAL B 136 34.038 19.848 15.717 1.00 46.79 C ATOM 2437 O VAL B 136 33.172 20.616 15.305 1.00 47.65 O ATOM 2438 N ILE B 137 34.471 19.848 16.974 1.00 45.80 N ATOM 2439 CA ILE B 137 33.979 20.790 17.975 1.00 41.88 C ATOM 2440 CB ILE B 137 34.586 20.487 19.352 1.00 43.18 C ATOM 2441 CG2 ILE B 137 34.525 21.719 20.259 1.00 40.79 C ATOM 2442 CG1 ILE B 137 33.879 19.285 19.989 1.00 43.56 C ATOM 2443 CD1 ILE B 137 34.569 18.761 21.260 1.00 49.33 C ATOM 2444 C ILE B 137 34.296 22.228 17.589 1.00 45.35 C ATOM 2445 O ILE B 137 33.403 23.083 17.573 1.00 43.72 O ATOM 2446 N ASP B 138 35.570 22.482 17.278 1.00 45.82 N ATOM 2447 CA ASP B 138 36.023 23.789 16.794 1.00 45.90 C ATOM 2448 CB ASP B 138 37.480 23.735 16.342 1.00 46.71 C ATOM 2449 CG ASP B 138 38.437 23.479 17.486 1.00 50.08 C ATOM 2450 OD1 ASP B 138 37.961 23.220 18.614 1.00 53.35 O ATOM 2451 OD2 ASP B 138 39.666 23.534 17.256 1.00 51.07 O ATOM 2452 C ASP B 138 35.178 24.261 15.627 1.00 48.51 C ATOM 2453 O ASP B 138 34.762 25.413 15.568 1.00 52.06 O ATOM 2454 N ASP B 139 34.920 23.370 14.687 1.00 46.87 N ATOM 2455 CA ASP B 139 34.096 23.754 13.571 1.00 43.14 C ATOM 2456 CB ASP B 139 34.283 22.818 12.380 1.00 36.90 C ATOM 2457 CG ASP B 139 33.158 22.951 11.380 1.00 45.32 C ATOM 2458 OD1 ASP B 139 33.270 23.802 10.470 1.00 44.79 O ATOM 2459 OD2 ASP B 139 32.136 22.238 11.536 1.00 47.81 O ATOM 2460 C ASP B 139 32.624 23.832 13.977 1.00 44.22 C ATOM 2461 O ASP B 139 31.870 24.625 13.417 1.00 48.03 O ATOM 2462 N ALA B 140 32.189 23.026 14.933 1.00 37.96 N ATOM 2463 CA ALA B 140 30.820 23.215 15.437 1.00 42.58 C ATOM 2464 CB ALA B 140 30.464 22.161 16.451 1.00 39.25 C ATOM 2465 C ALA B 140 30.627 24.627 16.024 1.00 37.23 C ATOM 2466 O ALA B 140 29.729 25.348 15.639 1.00 38.31 O ATOM 2467 N PHE B 141 31.481 25.036 16.944 1.00 44.23 N ATOM 2468 CA PHE B 141 31.399 26.403 17.451 1.00 44.73 C ATOM 2469 CB PHE B 141 32.452 26.611 18.520 1.00 41.79 C ATOM 2470 CG PHE B 141 32.239 25.779 19.737 1.00 50.31 C ATOM 2471 CD1 PHE B 141 30.974 25.644 20.286 1.00 44.88 C ATOM 2472 CD2 PHE B 141 33.302 25.149 20.359 1.00 53.74 C ATOM 2473 CE1 PHE B 141 30.773 24.894 21.422 1.00 43.47 C ATOM 2474 CE2 PHE B 141 33.099 24.394 21.508 1.00 49.33 C ATOM 2475 CZ PHE B 141 31.829 24.268 22.039 1.00 36.41 C ATOM 2476 C PHE B 141 31.588 27.451 16.342 1.00 44.73 C ATOM 2477 O PHE B 141 30.865 28.449 16.286 1.00 44.66 O ATOM 2478 N ALA B 142 32.564 27.220 15.470 1.00 32.97 N ATOM 2479 CA ALA B 142 32.870 28.132 14.360 1.00 38.54 C ATOM 2480 CB ALA B 142 33.921 27.497 13.403 1.00 30.62 C ATOM 2481 C ALA B 142 31.622 28.525 13.576 1.00 38.46 C ATOM 2482 O ALA B 142 31.325 29.712 13.430 1.00 39.38 O ATOM 2483 N ARG B 143 30.916 27.514 13.062 1.00 33.55 N ATOM 2484 CA ARG B 143 29.659 27.673 12.327 1.00 36.65 C ATOM 2485 CB ARG B 143 29.195 26.320 11.750 1.00 35.14 C ATOM 2486 CG ARG B 143 30.245 25.606 10.897 1.00 37.72 C ATOM 2487 CD ARG B 143 30.128 24.072 10.933 1.00 35.29 C ATOM 2488 NE ARG B 143 28.763 23.644 10.691 1.00 44.12 N ATOM 2489 CZ ARG B 143 28.015 23.016 11.598 1.00 53.32 C ATOM 2490 NH1 ARG B 143 28.539 22.707 12.785 1.00 52.29 N ATOM 2491 NH2 ARG B 143 26.752 22.690 11.327 1.00 41.29 N ATOM 2492 C ARG B 143 28.536 28.285 13.177 1.00 38.29 C ATOM 2493 O ARG B 143 27.765 29.109 12.686 1.00 36.85 O ATOM 2494 N ALA B 144 28.423 27.887 14.440 1.00 31.21 N ATOM 2495 CA ALA B 144 27.404 28.521 15.287 1.00 42.39 C ATOM 2496 CB ALA B 144 27.402 27.939 16.719 1.00 42.74 C ATOM 2497 C ALA B 144 27.609 30.039 15.326 1.00 42.18 C ATOM 2498 O ALA B 144 26.650 30.804 15.444 1.00 38.97 O ATOM 2499 N PHE B 145 28.873 30.456 15.246 1.00 42.18 N ATOM 2500 CA PHE B 145 29.223 31.870 15.228 1.00 36.63 C ATOM 2501 CB PHE B 145 30.671 32.094 15.657 1.00 39.89 C ATOM 2502 CG PHE B 145 30.851 32.174 17.157 1.00 40.77 C ATOM 2503 CD1 PHE B 145 30.193 33.141 17.893 1.00 37.31 C ATOM 2504 CD2 PHE B 145 31.696 31.297 17.824 1.00 43.42 C ATOM 2505 CE1 PHE B 145 30.355 33.218 19.271 1.00 44.18 C ATOM 2506 CE2 PHE B 145 31.865 31.373 19.201 1.00 40.50 C ATOM 2507 CZ PHE B 145 31.198 32.337 19.921 1.00 42.50 C ATOM 2508 C PHE B 145 28.954 32.478 13.873 1.00 39.76 C ATOM 2509 O PHE B 145 28.315 33.517 13.791 1.00 42.12 O ATOM 2510 N ALA B 146 29.421 31.821 12.813 1.00 39.28 N ATOM 2511 CA ALA B 146 29.077 32.230 11.459 1.00 36.57 C ATOM 2512 CB ALA B 146 29.392 31.131 10.493 1.00 30.77 C ATOM 2513 C ALA B 146 27.594 32.593 11.362 1.00 40.40 C ATOM 2514 O ALA B 146 27.213 33.507 10.633 1.00 37.27 O ATOM 2515 N LEU B 147 26.764 31.876 12.115 1.00 38.07 N ATOM 2516 CA LEU B 147 25.322 32.052 12.042 1.00 35.40 C ATOM 2517 CB LEU B 147 24.647 30.989 12.895 1.00 36.54 C ATOM 2518 CG LEU B 147 23.281 30.439 12.519 1.00 43.73 C ATOM 2519 CD1 LEU B 147 23.313 29.720 11.151 1.00 32.23 C ATOM 2520 CD2 LEU B 147 22.772 29.512 13.639 1.00 35.78 C ATOM 2521 C LEU B 147 24.903 33.462 12.464 1.00 39.12 C ATOM 2522 O LEU B 147 24.035 34.066 11.853 1.00 41.56 O ATOM 2523 N TRP B 148 25.551 33.988 13.501 1.00 40.82 N ATOM 2524 CA TRP B 148 25.323 35.353 13.969 1.00 36.38 C ATOM 2525 CB TRP B 148 25.625 35.430 15.475 1.00 45.02 C ATOM 2526 CG TRP B 148 24.677 34.592 16.297 1.00 41.66 C ATOM 2527 CD2 TRP B 148 23.291 34.864 16.536 1.00 32.30 C ATOM 2528 CE2 TRP B 148 22.789 33.816 17.331 1.00 35.29 C ATOM 2529 CE3 TRP B 148 22.420 35.887 16.139 1.00 37.95 C ATOM 2530 CD1 TRP B 148 24.957 33.421 16.947 1.00 41.88 C ATOM 2531 NE1 TRP B 148 23.829 32.957 17.584 1.00 35.92 N ATOM 2532 CZ2 TRP B 148 21.455 33.769 17.755 1.00 39.02 C ATOM 2533 CZ3 TRP B 148 21.084 35.836 16.557 1.00 41.39 C ATOM 2534 CH2 TRP B 148 20.623 34.785 17.366 1.00 34.28 C ATOM 2535 C TRP B 148 26.123 36.428 13.201 1.00 41.47 C ATOM 2536 O TRP B 148 25.636 37.547 12.995 1.00 41.59 O ATOM 2537 N SER B 149 27.349 36.096 12.787 1.00 35.70 N ATOM 2538 CA SER B 149 28.158 37.019 11.985 1.00 41.16 C ATOM 2539 CB SER B 149 29.321 36.301 11.260 1.00 43.67 C ATOM 2540 OG SER B 149 30.109 35.478 12.106 1.00 47.58 O ATOM 2541 C SER B 149 27.286 37.658 10.917 1.00 39.00 C ATOM 2542 O SER B 149 27.248 38.874 10.779 1.00 41.47 O ATOM 2543 N ALA B 150 26.594 36.813 10.160 1.00 37.36 N ATOM 2544 CA ALA B 150 25.899 37.235 8.956 1.00 37.94 C ATOM 2545 CB ALA B 150 25.360 36.034 8.228 1.00 38.47 C ATOM 2546 C ALA B 150 24.794 38.254 9.194 1.00 41.07 C ATOM 2547 O ALA B 150 24.509 39.071 8.307 1.00 38.81 O ATOM 2548 N VAL B 151 24.174 38.208 10.378 1.00 43.33 N ATOM 2549 CA VAL B 151 23.034 39.097 10.681 1.00 48.91 C ATOM 2550 CB VAL B 151 21.782 38.323 11.143 1.00 40.98 C ATOM 2551 CG1 VAL B 151 21.211 37.534 9.978 1.00 42.92 C ATOM 2552 CG2 VAL B 151 22.134 37.393 12.267 1.00 38.84 C ATOM 2553 C VAL B 151 23.399 40.161 11.698 1.00 43.37 C ATOM 2554 O VAL B 151 22.578 40.584 12.507 1.00 42.70 O ATOM 2555 N THR B 152 24.641 40.613 11.616 1.00 47.40 N ATOM 2556 CA THR B 152 25.211 41.458 12.650 1.00 47.88 C ATOM 2557 CB THR B 152 25.653 40.580 13.828 1.00 38.22 C ATOM 2558 OG1 THR B 152 24.516 40.263 14.632 1.00 41.99 O ATOM 2559 CG2 THR B 152 26.590 41.300 14.664 1.00 46.10 C ATOM 2560 C THR B 152 26.395 42.278 12.119 1.00 49.13 C ATOM 2561 O THR B 152 27.029 41.917 11.111 1.00 46.38 O ATOM 2562 N PRO B 153 26.669 43.412 12.770 1.00 48.99 N ATOM 2563 CD PRO B 153 25.619 44.193 13.439 1.00 52.39 C ATOM 2564 CA PRO B 153 27.901 44.190 12.555 1.00 52.22 C ATOM 2565 CB PRO B 153 27.537 45.572 13.102 1.00 52.87 C ATOM 2566 CG PRO B 153 26.012 45.598 13.107 1.00 57.75 C ATOM 2567 C PRO B 153 29.109 43.617 13.322 1.00 52.65 C ATOM 2568 O PRO B 153 30.187 44.209 13.316 1.00 52.62 O ATOM 2569 N LEU B 154 28.917 42.473 13.972 1.00 47.57 N ATOM 2570 CA LEU B 154 29.976 41.828 14.747 1.00 56.79 C ATOM 2571 CB LEU B 154 29.421 41.133 16.000 1.00 49.00 C ATOM 2572 CG LEU B 154 28.426 41.904 16.878 1.00 52.80 C ATOM 2573 CD1 LEU B 154 28.022 41.133 18.146 1.00 44.26 C ATOM 2574 CD2 LEU B 154 28.964 43.282 17.209 1.00 53.90 C ATOM 2575 C LEU B 154 30.714 40.797 13.909 1.00 55.83 C ATOM 2576 O LEU B 154 30.192 40.313 12.902 1.00 51.73 O ATOM 2577 N THR B 155 31.921 40.454 14.352 1.00 45.67 N ATOM 2578 CA THR B 155 32.683 39.376 13.739 1.00 49.59 C ATOM 2579 CB THR B 155 33.717 39.899 12.716 1.00 54.49 C ATOM 2580 OG1 THR B 155 34.876 40.399 13.401 1.00 45.06 O ATOM 2581 CG2 THR B 155 33.111 41.009 11.881 1.00 55.61 C ATOM 2582 C THR B 155 33.408 38.638 14.851 1.00 50.68 C ATOM 2583 O THR B 155 33.709 39.221 15.902 1.00 53.32 O ATOM 2584 N PHE B 156 33.696 37.365 14.624 1.00 42.59 N ATOM 2585 CA PHE B 156 34.262 36.527 15.666 1.00 39.96 C ATOM 2586 CB PHE B 156 33.304 35.395 16.017 1.00 37.92 C ATOM 2587 CG PHE B 156 31.924 35.884 16.288 1.00 43.08 C ATOM 2588 CD1 PHE B 156 31.051 36.124 15.234 1.00 43.49 C ATOM 2589 CD2 PHE B 156 31.522 36.190 17.577 1.00 38.99 C ATOM 2590 CE1 PHE B 156 29.790 36.613 15.465 1.00 44.62 C ATOM 2591 CE2 PHE B 156 30.259 36.684 17.820 1.00 40.31 C ATOM 2592 CZ PHE B 156 29.392 36.901 16.768 1.00 48.27 C ATOM 2593 C PHE B 156 35.566 36.004 15.176 1.00 43.57 C ATOM 2594 O PHE B 156 35.683 35.570 14.032 1.00 44.94 O ATOM 2595 N THR B 157 36.568 36.113 16.028 1.00 39.48 N ATOM 2596 CA THR B 157 37.826 35.464 15.777 1.00 42.41 C ATOM 2597 CB THR B 157 38.958 36.469 15.546 1.00 38.47 C ATOM 2598 OG1 THR B 157 39.296 37.106 16.777 1.00 54.30 O ATOM 2599 CG2 THR B 157 38.504 37.544 14.592 1.00 50.07 C ATOM 2600 C THR B 157 38.087 34.610 17.004 1.00 46.17 C ATOM 2601 O THR B 157 37.925 35.062 18.156 1.00 37.93 O ATOM 2602 N ARG B 158 38.449 33.361 16.744 1.00 38.99 N ATOM 2603 CA ARG B 158 38.887 32.471 17.785 1.00 41.15 C ATOM 2604 CB ARG B 158 39.138 31.082 17.205 1.00 42.10 C ATOM 2605 CG ARG B 158 39.307 30.007 18.237 1.00 47.12 C ATOM 2606 CD ARG B 158 39.304 28.649 17.594 1.00 41.09 C ATOM 2607 NE ARG B 158 39.870 27.665 18.500 1.00 47.78 N ATOM 2608 CZ ARG B 158 40.263 26.455 18.128 1.00 48.00 C ATOM 2609 NH1 ARG B 158 40.146 26.088 16.863 1.00 45.99 N ATOM 2610 NH2 ARG B 158 40.782 25.618 19.018 1.00 50.44 N ATOM 2611 C ARG B 158 40.180 33.070 18.296 1.00 41.36 C ATOM 2612 O ARG B 158 40.970 33.581 17.511 1.00 41.75 O ATOM 2613 N VAL B 159 40.382 33.045 19.603 1.00 39.91 N ATOM 2614 CA VAL B 159 41.652 33.472 20.185 1.00 44.14 C ATOM 2615 CB VAL B 159 41.495 34.834 20.864 1.00 43.08 C ATOM 2616 CG1 VAL B 159 42.708 35.178 21.681 1.00 49.76 C ATOM 2617 CG2 VAL B 159 41.240 35.909 19.790 1.00 41.83 C ATOM 2618 C VAL B 159 42.175 32.366 21.111 1.00 38.34 C ATOM 2619 O VAL B 159 41.502 31.363 21.315 1.00 45.28 O ATOM 2620 N TYR B 160 43.377 32.498 21.635 1.00 42.84 N ATOM 2621 CA TYR B 160 43.908 31.415 22.464 1.00 46.30 C ATOM 2622 CB TYR B 160 44.995 30.641 21.703 1.00 41.91 C ATOM 2623 CG TYR B 160 44.435 29.980 20.467 1.00 36.51 C ATOM 2624 CD1 TYR B 160 44.287 30.692 19.293 1.00 42.24 C ATOM 2625 CE1 TYR B 160 43.737 30.111 18.161 1.00 43.41 C ATOM 2626 CD2 TYR B 160 43.997 28.665 20.493 1.00 40.59 C ATOM 2627 CE2 TYR B 160 43.436 28.068 19.371 1.00 39.73 C ATOM 2628 CZ TYR B 160 43.313 28.799 18.203 1.00 44.58 C ATOM 2629 OH TYR B 160 42.782 28.216 17.063 1.00 48.09 O ATOM 2630 C TYR B 160 44.354 31.804 23.883 1.00 42.41 C ATOM 2631 O TYR B 160 45.160 31.111 24.487 1.00 42.25 O ATOM 2632 N SER B 161 43.795 32.874 24.436 1.00 45.05 N ATOM 2633 CA SER B 161 44.065 33.206 25.849 1.00 50.83 C ATOM 2634 CB SER B 161 45.028 34.387 25.957 1.00 46.11 C ATOM 2635 OG SER B 161 44.544 35.500 25.211 1.00 52.41 O ATOM 2636 C SER B 161 42.811 33.548 26.642 1.00 46.38 C ATOM 2637 O SER B 161 41.805 33.971 26.079 1.00 45.28 O ATOM 2638 N ARG B 162 42.896 33.385 27.956 1.00 52.45 N ATOM 2639 CA ARG B 162 41.860 33.844 28.879 1.00 51.61 C ATOM 2640 CB ARG B 162 42.469 34.069 30.270 1.00 49.34 C ATOM 2641 CG ARG B 162 42.309 32.890 31.244 1.00 65.82 C ATOM 2642 CD ARG B 162 43.603 32.582 32.018 1.00 49.54 C ATOM 2643 NE ARG B 162 44.583 31.981 31.122 1.00 59.77 N ATOM 2644 CZ ARG B 162 44.723 30.672 30.944 1.00 59.68 C ATOM 2645 NH1 ARG B 162 43.957 29.828 31.631 1.00 47.87 N ATOM 2646 NH2 ARG B 162 45.630 30.210 30.081 1.00 54.39 N ATOM 2647 C ARG B 162 41.197 35.138 28.384 1.00 53.50 C ATOM 2648 O ARG B 162 39.988 35.334 28.551 1.00 53.34 O ATOM 2649 N ASP B 163 41.997 36.007 27.768 1.00 43.29 N ATOM 2650 CA ASP B 163 41.545 37.317 27.288 1.00 56.43 C ATOM 2651 CB ASP B 163 42.594 37.909 26.329 1.00 60.87 C ATOM 2652 CG ASP B 163 43.042 39.310 26.735 1.00 65.30 C ATOM 2653 OD1 ASP B 163 44.020 39.826 26.145 1.00 60.90 O ATOM 2654 OD2 ASP B 163 42.409 39.897 27.643 1.00 72.49 O ATOM 2655 C ASP B 163 40.129 37.383 26.646 1.00 59.61 C ATOM 2656 O ASP B 163 39.329 38.249 26.995 1.00 60.23 O ATOM 2657 N ALA B 164 39.844 36.472 25.715 1.00 55.26 N ATOM 2658 CA ALA B 164 38.604 36.467 24.908 1.00 50.58 C ATOM 2659 CB ALA B 164 38.414 35.083 24.242 1.00 44.38 C ATOM 2660 C ALA B 164 37.290 36.891 25.587 1.00 49.22 C ATOM 2661 O ALA B 164 36.920 36.350 26.620 1.00 47.88 O ATOM 2662 N ASP B 165 36.582 37.833 24.962 1.00 50.27 N ATOM 2663 CA ASP B 165 35.216 38.196 25.342 1.00 44.63 C ATOM 2664 CB ASP B 165 34.498 38.953 24.206 1.00 45.52 C ATOM 2665 CG ASP B 165 35.289 40.165 23.676 1.00 51.92 C ATOM 2666 OD1 ASP B 165 35.223 40.425 22.450 1.00 50.47 O ATOM 2667 OD2 ASP B 165 35.962 40.862 24.464 1.00 45.35 O ATOM 2668 C ASP B 165 34.395 36.944 25.671 1.00 44.86 C ATOM 2669 O ASP B 165 33.687 36.883 26.674 1.00 39.38 O ATOM 2670 N ILE B 166 34.476 35.940 24.809 1.00 45.32 N ATOM 2671 CA ILE B 166 33.668 34.749 25.013 1.00 47.66 C ATOM 2672 CB ILE B 166 32.779 34.420 23.805 1.00 47.15 C ATOM 2673 CG2 ILE B 166 32.051 33.119 24.057 1.00 39.55 C ATOM 2674 CG1 ILE B 166 31.801 35.560 23.528 1.00 45.07 C ATOM 2675 CD1 ILE B 166 30.838 35.263 22.393 1.00 39.87 C ATOM 2676 C ILE B 166 34.510 33.529 25.327 1.00 46.59 C ATOM 2677 O ILE B 166 35.129 32.931 24.438 1.00 41.09 O ATOM 2678 N VAL B 167 34.528 33.165 26.605 1.00 46.44 N ATOM 2679 CA VAL B 167 35.243 31.985 27.033 1.00 45.54 C ATOM 2680 CB VAL B 167 35.837 32.153 28.434 1.00 47.68 C ATOM 2681 CG1 VAL B 167 36.183 30.799 29.035 1.00 45.14 C ATOM 2682 CG2 VAL B 167 37.049 33.040 28.365 1.00 44.51 C ATOM 2683 C VAL B 167 34.253 30.849 27.019 1.00 47.23 C ATOM 2684 O VAL B 167 33.202 30.933 27.648 1.00 47.05 O ATOM 2685 N ILE B 168 34.592 29.798 26.280 1.00 43.73 N ATOM 2686 CA ILE B 168 33.720 28.653 26.091 1.00 40.59 C ATOM 2687 CB ILE B 168 33.640 28.285 24.585 1.00 43.09 C ATOM 2688 CG2 ILE B 168 33.041 26.896 24.400 1.00 35.97 C ATOM 2689 CG1 ILE B 168 32.858 29.367 23.835 1.00 39.54 C ATOM 2690 CD1 ILE B 168 32.964 29.288 22.340 1.00 40.13 C ATOM 2691 C ILE B 168 34.263 27.487 26.889 1.00 38.60 C ATOM 2692 O ILE B 168 35.482 27.272 26.927 1.00 47.70 O ATOM 2693 N GLN B 169 33.388 26.719 27.520 1.00 34.54 N ATOM 2694 CA GLN B 169 33.878 25.711 28.467 1.00 40.05 C ATOM 2695 CB GLN B 169 34.188 26.389 29.813 1.00 41.85 C ATOM 2696 CG GLN B 169 34.307 25.495 31.036 1.00 46.92 C ATOM 2697 CD GLN B 169 34.463 26.328 32.306 1.00 51.78 C ATOM 2698 OE1 GLN B 169 34.104 25.900 33.407 1.00 46.07 O ATOM 2699 NE2 GLN B 169 34.996 27.539 32.149 1.00 56.59 N ATOM 2700 C GLN B 169 32.965 24.500 28.642 1.00 40.63 C ATOM 2701 O GLN B 169 31.747 24.617 28.669 1.00 49.42 O ATOM 2702 N PHE B 170 33.559 23.325 28.744 1.00 44.35 N ATOM 2703 CA PHE B 170 32.780 22.132 29.010 1.00 49.07 C ATOM 2704 CB PHE B 170 33.313 20.961 28.209 1.00 46.98 C ATOM 2705 CG PHE B 170 32.917 20.984 26.785 1.00 46.12 C ATOM 2706 CD1 PHE B 170 33.660 21.685 25.860 1.00 50.30 C ATOM 2707 CD2 PHE B 170 31.799 20.301 26.361 1.00 48.43 C ATOM 2708 CE1 PHE B 170 33.299 21.698 24.527 1.00 45.87 C ATOM 2709 CE2 PHE B 170 31.438 20.303 25.044 1.00 46.67 C ATOM 2710 CZ PHE B 170 32.191 21.007 24.119 1.00 44.42 C ATOM 2711 C PHE B 170 32.919 21.836 30.484 1.00 45.77 C ATOM 2712 O PHE B 170 34.008 21.971 31.021 1.00 47.32 O ATOM 2713 N GLY B 171 31.824 21.450 31.131 1.00 45.24 N ATOM 2714 CA GLY B 171 31.828 21.182 32.565 1.00 50.33 C ATOM 2715 C GLY B 171 30.826 20.107 32.926 1.00 51.23 C ATOM 2716 O GLY B 171 30.096 19.640 32.061 1.00 54.72 O ATOM 2717 N VAL B 172 30.758 19.723 34.193 1.00 50.00 N ATOM 2718 CA VAL B 172 29.923 18.593 34.568 1.00 49.97 C ATOM 2719 CB VAL B 172 30.790 17.395 34.964 1.00 57.79 C ATOM 2720 CG1 VAL B 172 30.058 16.509 35.957 1.00 59.47 C ATOM 2721 CG2 VAL B 172 31.216 16.620 33.706 1.00 48.17 C ATOM 2722 C VAL B 172 28.864 18.881 35.644 1.00 60.01 C ATOM 2723 O VAL B 172 27.659 18.688 35.414 1.00 63.69 O ATOM 2724 N ALA B 173 29.293 19.330 36.816 1.00 50.32 N ATOM 2725 CA ALA B 173 28.337 19.660 37.865 1.00 44.24 C ATOM 2726 CB ALA B 173 28.433 18.678 39.002 1.00 40.20 C ATOM 2727 C ALA B 173 28.617 21.076 38.336 1.00 47.33 C ATOM 2728 O ALA B 173 28.365 22.020 37.598 1.00 43.53 O ATOM 2729 N GLU B 174 29.153 21.234 39.547 1.00 45.48 N ATOM 2730 CA GLU B 174 29.634 22.550 39.968 1.00 48.12 C ATOM 2731 CB GLU B 174 29.926 22.604 41.478 1.00 47.78 C ATOM 2732 CG GLU B 174 29.132 23.667 42.258 1.00 43.07 C ATOM 2733 CD GLU B 174 29.432 25.112 41.849 1.00 50.86 C ATOM 2734 OE1 GLU B 174 30.539 25.405 41.334 1.00 51.30 O ATOM 2735 OE2 GLU B 174 28.549 25.971 42.067 1.00 54.43 O ATOM 2736 C GLU B 174 30.911 22.815 39.179 1.00 47.74 C ATOM 2737 O GLU B 174 31.951 22.205 39.442 1.00 47.90 O ATOM 2738 N HIS B 175 30.838 23.695 38.190 1.00 46.43 N ATOM 2739 CA HIS B 175 32.013 23.921 37.355 1.00 51.77 C ATOM 2740 CB HIS B 175 31.691 23.828 35.851 1.00 50.72 C ATOM 2741 CG HIS B 175 30.315 24.286 35.497 1.00 42.77 C ATOM 2742 CD2 HIS B 175 29.887 25.309 34.720 1.00 44.80 C ATOM 2743 ND1 HIS B 175 29.182 23.657 35.958 1.00 50.90 N ATOM 2744 CE1 HIS B 175 28.112 24.269 35.485 1.00 51.82 C ATOM 2745 NE2 HIS B 175 28.512 25.273 34.727 1.00 52.15 N ATOM 2746 C HIS B 175 32.709 25.222 37.713 1.00 50.14 C ATOM 2747 O HIS B 175 33.626 25.654 37.020 1.00 51.80 O ATOM 2748 N GLY B 176 32.265 25.837 38.805 1.00 52.97 N ATOM 2749 CA GLY B 176 32.970 26.971 39.370 1.00 49.35 C ATOM 2750 C GLY B 176 32.364 28.316 39.036 1.00 55.22 C ATOM 2751 O GLY B 176 33.094 29.281 38.812 1.00 55.51 O ATOM 2752 N ASP B 177 31.036 28.394 39.002 1.00 50.37 N ATOM 2753 CA ASP B 177 30.384 29.661 38.719 1.00 41.44 C ATOM 2754 CB ASP B 177 30.270 29.885 37.212 1.00 45.44 C ATOM 2755 CG ASP B 177 29.129 29.115 36.581 1.00 45.46 C ATOM 2756 OD1 ASP B 177 28.604 28.148 37.180 1.00 46.45 O ATOM 2757 OD2 ASP B 177 28.761 29.494 35.452 1.00 47.77 O ATOM 2758 C ASP B 177 29.024 29.816 39.396 1.00 48.73 C ATOM 2759 O ASP B 177 28.288 30.780 39.118 1.00 47.25 O ATOM 2760 N GLY B 178 28.704 28.875 40.284 1.00 49.40 N ATOM 2761 CA GLY B 178 27.518 28.976 41.122 1.00 48.06 C ATOM 2762 C GLY B 178 26.244 28.601 40.382 1.00 51.59 C ATOM 2763 O GLY B 178 25.150 28.952 40.810 1.00 52.16 O ATOM 2764 N TYR B 179 26.391 27.903 39.259 1.00 51.51 N ATOM 2765 CA TYR B 179 25.247 27.382 38.520 1.00 49.71 C ATOM 2766 CB TYR B 179 24.874 28.311 37.362 1.00 43.33 C ATOM 2767 CG TYR B 179 24.265 29.635 37.791 1.00 47.22 C ATOM 2768 CD1 TYR B 179 25.058 30.759 38.007 1.00 50.29 C ATOM 2769 CE1 TYR B 179 24.505 31.979 38.388 1.00 45.13 C ATOM 2770 CD2 TYR B 179 22.899 29.767 37.965 1.00 43.61 C ATOM 2771 CE2 TYR B 179 22.340 30.989 38.340 1.00 48.53 C ATOM 2772 CZ TYR B 179 23.147 32.086 38.549 1.00 50.90 C ATOM 2773 OH TYR B 179 22.580 33.284 38.924 1.00 53.58 O ATOM 2774 C TYR B 179 25.601 25.995 38.007 1.00 48.24 C ATOM 2775 O TYR B 179 25.953 25.825 36.845 1.00 49.75 O ATOM 2776 N PRO B 180 25.529 24.992 38.887 1.00 45.68 N ATOM 2777 CD PRO B 180 24.882 24.996 40.208 1.00 49.14 C ATOM 2778 CA PRO B 180 25.996 23.661 38.502 1.00 44.76 C ATOM 2779 CB PRO B 180 25.899 22.845 39.804 1.00 43.44 C ATOM 2780 CG PRO B 180 25.504 23.821 40.885 1.00 51.17 C ATOM 2781 C PRO B 180 25.077 23.038 37.468 1.00 47.80 C ATOM 2782 O PRO B 180 23.865 23.267 37.502 1.00 55.51 O ATOM 2783 N PHE B 181 25.651 22.256 36.563 1.00 47.21 N ATOM 2784 CA PHE B 181 24.864 21.402 35.701 1.00 50.02 C ATOM 2785 CB PHE B 181 25.691 20.947 34.512 1.00 51.95 C ATOM 2786 CG PHE B 181 25.954 22.038 33.528 1.00 48.50 C ATOM 2787 CD1 PHE B 181 24.914 22.826 33.067 1.00 47.28 C ATOM 2788 CD2 PHE B 181 27.233 22.277 33.063 1.00 49.14 C ATOM 2789 CE1 PHE B 181 25.139 23.833 32.146 1.00 44.71 C ATOM 2790 CE2 PHE B 181 27.470 23.276 32.152 1.00 46.17 C ATOM 2791 CZ PHE B 181 26.417 24.058 31.693 1.00 46.26 C ATOM 2792 C PHE B 181 24.361 20.221 36.509 1.00 48.80 C ATOM 2793 O PHE B 181 24.868 19.947 37.599 1.00 45.12 O ATOM 2794 N ASP B 182 23.352 19.541 35.973 1.00 54.26 N ATOM 2795 CA ASP B 182 22.511 18.640 36.768 1.00 51.42 C ATOM 2796 CB ASP B 182 21.021 19.020 36.642 1.00 41.18 C ATOM 2797 CG ASP B 182 20.438 18.703 35.253 1.00 53.65 C ATOM 2798 OD1 ASP B 182 21.145 18.897 34.244 1.00 51.66 O ATOM 2799 OD2 ASP B 182 19.271 18.257 35.163 1.00 53.92 O ATOM 2800 C ASP B 182 22.709 17.194 36.352 1.00 52.76 C ATOM 2801 O ASP B 182 21.815 16.364 36.502 1.00 56.83 O ATOM 2802 N GLY B 183 23.886 16.881 35.842 1.00 48.28 N ATOM 2803 CA GLY B 183 24.106 15.553 35.324 1.00 54.74 C ATOM 2804 C GLY B 183 23.546 15.400 33.921 1.00 58.43 C ATOM 2805 O GLY B 183 23.816 16.198 33.029 1.00 59.65 O ATOM 2806 N LYS B 184 22.748 14.368 33.726 1.00 53.68 N ATOM 2807 CA LYS B 184 22.341 13.962 32.397 1.00 53.55 C ATOM 2808 CB LYS B 184 22.506 12.446 32.293 1.00 53.83 C ATOM 2809 CG LYS B 184 21.557 11.752 31.348 1.00 57.21 C ATOM 2810 CD LYS B 184 21.399 10.292 31.751 1.00 60.16 C ATOM 2811 CE LYS B 184 20.555 9.543 30.750 1.00 61.42 C ATOM 2812 NZ LYS B 184 21.140 9.714 29.392 1.00 64.94 N ATOM 2813 C LYS B 184 20.907 14.383 32.065 1.00 54.48 C ATOM 2814 O LYS B 184 19.990 14.112 32.840 1.00 58.34 O ATOM 2815 N ASP B 185 20.726 15.076 30.941 1.00 50.25 N ATOM 2816 CA ASP B 185 19.392 15.312 30.365 1.00 53.85 C ATOM 2817 CB ASP B 185 18.608 13.995 30.280 1.00 55.73 C ATOM 2818 CG ASP B 185 19.205 13.045 29.292 1.00 54.19 C ATOM 2819 OD1 ASP B 185 19.845 13.550 28.359 1.00 43.11 O ATOM 2820 OD2 ASP B 185 19.046 11.815 29.450 1.00 60.16 O ATOM 2821 C ASP B 185 18.499 16.335 31.057 1.00 58.06 C ATOM 2822 O ASP B 185 17.268 16.216 31.012 1.00 58.43 O ATOM 2823 N GLY B 186 19.084 17.328 31.708 1.00 54.05 N ATOM 2824 CA GLY B 186 18.258 18.325 32.363 1.00 50.65 C ATOM 2825 C GLY B 186 18.436 19.614 31.611 1.00 51.53 C ATOM 2826 O GLY B 186 17.932 19.778 30.500 1.00 46.01 O ATOM 2827 N LEU B 187 19.179 20.531 32.212 1.00 53.10 N ATOM 2828 CA LEU B 187 19.711 21.637 31.440 1.00 53.17 C ATOM 2829 CB LEU B 187 19.917 22.868 32.324 1.00 47.91 C ATOM 2830 CG LEU B 187 20.416 22.602 33.735 1.00 51.87 C ATOM 2831 CD1 LEU B 187 21.867 22.175 33.677 1.00 58.23 C ATOM 2832 CD2 LEU B 187 20.244 23.838 34.620 1.00 50.75 C ATOM 2833 C LEU B 187 21.005 21.180 30.729 1.00 54.14 C ATOM 2834 O LEU B 187 21.845 20.481 31.311 1.00 53.20 O ATOM 2835 N LEU B 188 21.143 21.571 29.468 1.00 47.16 N ATOM 2836 CA LEU B 188 22.213 21.101 28.602 1.00 40.11 C ATOM 2837 CB LEU B 188 21.674 20.999 27.176 1.00 40.92 C ATOM 2838 CG LEU B 188 20.422 20.129 26.980 1.00 39.12 C ATOM 2839 CD1 LEU B 188 19.842 20.294 25.595 1.00 47.00 C ATOM 2840 CD2 LEU B 188 20.743 18.669 27.195 1.00 42.65 C ATOM 2841 C LEU B 188 23.413 22.046 28.635 1.00 42.63 C ATOM 2842 O LEU B 188 24.569 21.620 28.492 1.00 45.19 O ATOM 2843 N ALA B 189 23.136 23.336 28.805 1.00 38.80 N ATOM 2844 CA ALA B 189 24.186 24.350 28.830 1.00 42.55 C ATOM 2845 CB ALA B 189 24.987 24.330 27.510 1.00 41.22 C ATOM 2846 C ALA B 189 23.629 25.752 29.135 1.00 43.73 C ATOM 2847 O ALA B 189 22.411 25.918 29.283 1.00 40.33 O ATOM 2848 N HIS B 190 24.515 26.744 29.260 1.00 40.60 N ATOM 2849 CA HIS B 190 24.092 28.130 29.492 1.00 44.48 C ATOM 2850 CB HIS B 190 23.537 28.345 30.909 1.00 39.24 C ATOM 2851 CG HIS B 190 24.411 27.811 31.998 1.00 43.97 C ATOM 2852 CD2 HIS B 190 25.728 27.992 32.263 1.00 47.51 C ATOM 2853 ND1 HIS B 190 23.935 26.975 32.987 1.00 45.16 N ATOM 2854 CE1 HIS B 190 24.921 26.665 33.813 1.00 43.06 C ATOM 2855 NE2 HIS B 190 26.019 27.269 33.396 1.00 42.91 N ATOM 2856 C HIS B 190 25.173 29.168 29.177 1.00 42.83 C ATOM 2857 O HIS B 190 26.229 28.836 28.653 1.00 39.94 O ATOM 2858 N ALA B 191 24.890 30.429 29.497 1.00 38.14 N ATOM 2859 CA ALA B 191 25.775 31.529 29.156 1.00 42.01 C ATOM 2860 CB ALA B 191 25.705 31.840 27.649 1.00 41.11 C ATOM 2861 C ALA B 191 25.372 32.750 29.962 1.00 45.68 C ATOM 2862 O ALA B 191 24.291 32.785 30.554 1.00 43.97 O ATOM 2863 N PHE B 192 26.239 33.756 29.959 1.00 45.58 N ATOM 2864 CA PHE B 192 25.978 35.003 30.655 1.00 43.55 C ATOM 2865 CB PHE B 192 27.116 35.311 31.626 1.00 45.45 C ATOM 2866 CG PHE B 192 27.387 34.210 32.621 1.00 49.65 C ATOM 2867 CD1 PHE B 192 26.863 34.269 33.897 1.00 50.50 C ATOM 2868 CD2 PHE B 192 28.169 33.120 32.277 1.00 50.65 C ATOM 2869 CE1 PHE B 192 27.109 33.272 34.805 1.00 45.53 C ATOM 2870 CE2 PHE B 192 28.418 32.117 33.186 1.00 49.79 C ATOM 2871 CZ PHE B 192 27.887 32.191 34.447 1.00 46.35 C ATOM 2872 C PHE B 192 25.890 36.098 29.614 1.00 45.28 C ATOM 2873 O PHE B 192 26.533 36.006 28.586 1.00 39.26 O ATOM 2874 N PRO B 193 25.092 37.150 29.878 1.00 46.19 N ATOM 2875 CD PRO B 193 24.435 37.521 31.132 1.00 46.14 C ATOM 2876 CA PRO B 193 24.980 38.215 28.881 1.00 48.37 C ATOM 2877 CB PRO B 193 24.004 39.210 29.531 1.00 45.06 C ATOM 2878 CG PRO B 193 23.457 38.540 30.685 1.00 48.62 C ATOM 2879 C PRO B 193 26.332 38.895 28.635 1.00 45.66 C ATOM 2880 O PRO B 193 27.284 38.645 29.359 1.00 43.50 O ATOM 2881 N PRO B 194 26.414 39.745 27.601 1.00 49.70 N ATOM 2882 CD PRO B 194 25.437 39.879 26.511 1.00 46.95 C ATOM 2883 CA PRO B 194 27.623 40.537 27.358 1.00 48.78 C ATOM 2884 CB PRO B 194 27.223 41.419 26.174 1.00 48.92 C ATOM 2885 CG PRO B 194 26.210 40.609 25.445 1.00 48.47 C ATOM 2886 C PRO B 194 27.950 41.393 28.571 1.00 51.18 C ATOM 2887 O PRO B 194 27.087 41.608 29.421 1.00 49.25 O ATOM 2888 N GLY B 195 29.179 41.885 28.639 1.00 46.50 N ATOM 2889 CA GLY B 195 29.650 42.585 29.812 1.00 50.47 C ATOM 2890 C GLY B 195 30.954 41.962 30.263 1.00 56.57 C ATOM 2891 O GLY B 195 31.405 40.984 29.668 1.00 56.94 O ATOM 2892 N PRO B 196 31.566 42.529 31.311 1.00 53.57 N ATOM 2893 CD PRO B 196 30.991 43.735 31.935 1.00 58.62 C ATOM 2894 CA PRO B 196 32.874 42.179 31.886 1.00 51.48 C ATOM 2895 CB PRO B 196 32.928 43.036 33.155 1.00 53.80 C ATOM 2896 CG PRO B 196 32.087 44.220 32.847 1.00 60.70 C ATOM 2897 C PRO B 196 33.105 40.706 32.264 1.00 53.61 C ATOM 2898 O PRO B 196 32.178 39.896 32.312 1.00 46.46 O ATOM 2899 N GLY B 197 34.377 40.393 32.527 1.00 55.28 N ATOM 2900 CA GLY B 197 34.805 39.158 33.167 1.00 46.50 C ATOM 2901 C GLY B 197 34.185 37.863 32.684 1.00 48.19 C ATOM 2902 O GLY B 197 34.472 37.398 31.582 1.00 41.17 O ATOM 2903 N ILE B 198 33.347 37.264 33.521 1.00 44.97 N ATOM 2904 CA ILE B 198 32.744 35.998 33.152 1.00 48.64 C ATOM 2905 CB ILE B 198 32.395 35.145 34.372 1.00 47.01 C ATOM 2906 CG2 ILE B 198 31.140 35.660 35.041 1.00 42.61 C ATOM 2907 CG1 ILE B 198 32.267 33.673 33.968 1.00 50.50 C ATOM 2908 CD1 ILE B 198 31.770 32.779 35.096 1.00 54.16 C ATOM 2909 C ILE B 198 31.524 36.194 32.246 1.00 52.60 C ATOM 2910 O ILE B 198 31.172 35.303 31.464 1.00 51.85 O ATOM 2911 N GLN B 199 30.893 37.363 32.328 1.00 49.89 N ATOM 2912 CA GLN B 199 29.816 37.671 31.389 1.00 50.97 C ATOM 2913 CB GLN B 199 29.303 39.105 31.567 1.00 50.45 C ATOM 2914 CG GLN B 199 28.467 39.316 32.821 1.00 42.84 C ATOM 2915 CD GLN B 199 28.166 40.782 33.093 1.00 51.99 C ATOM 2916 OE1 GLN B 199 27.507 41.472 32.294 1.00 48.74 O ATOM 2917 NE2 GLN B 199 28.645 41.267 34.231 1.00 54.54 N ATOM 2918 C GLN B 199 30.343 37.453 29.979 1.00 49.34 C ATOM 2919 O GLN B 199 31.460 37.838 29.670 1.00 47.66 O ATOM 2920 N GLY B 200 29.540 36.819 29.132 1.00 53.57 N ATOM 2921 CA GLY B 200 29.956 36.485 27.780 1.00 44.50 C ATOM 2922 C GLY B 200 30.247 35.001 27.645 1.00 47.43 C ATOM 2923 O GLY B 200 30.034 34.414 26.585 1.00 50.95 O ATOM 2924 N ASP B 201 30.738 34.391 28.722 1.00 47.30 N ATOM 2925 CA ASP B 201 31.079 32.966 28.710 1.00 50.73 C ATOM 2926 CB ASP B 201 31.519 32.498 30.106 1.00 48.14 C ATOM 2927 CG ASP B 201 32.996 32.713 30.372 1.00 54.77 C ATOM 2928 OD1 ASP B 201 33.628 33.486 29.620 1.00 53.04 O ATOM 2929 OD2 ASP B 201 33.523 32.103 31.344 1.00 63.32 O ATOM 2930 C ASP B 201 29.907 32.086 28.284 1.00 49.83 C ATOM 2931 O ASP B 201 28.736 32.388 28.577 1.00 50.33 O ATOM 2932 N ALA B 202 30.226 30.973 27.640 1.00 38.84 N ATOM 2933 CA ALA B 202 29.231 29.938 27.395 1.00 45.51 C ATOM 2934 CB ALA B 202 28.935 29.833 25.908 1.00 43.79 C ATOM 2935 C ALA B 202 29.718 28.601 27.929 1.00 43.31 C ATOM 2936 O ALA B 202 30.811 28.178 27.580 1.00 48.48 O ATOM 2937 N HIS B 203 28.916 27.932 28.755 1.00 36.37 N ATOM 2938 CA HIS B 203 29.319 26.635 29.328 1.00 43.55 C ATOM 2939 CB HIS B 203 29.350 26.708 30.841 1.00 42.80 C ATOM 2940 CG HIS B 203 30.248 27.776 31.367 1.00 43.82 C ATOM 2941 CD2 HIS B 203 31.274 28.438 30.789 1.00 45.53 C ATOM 2942 ND1 HIS B 203 30.125 28.298 32.637 1.00 44.98 N ATOM 2943 CE1 HIS B 203 31.041 29.228 32.820 1.00 49.72 C ATOM 2944 NE2 HIS B 203 31.752 29.333 31.712 1.00 47.89 N ATOM 2945 C HIS B 203 28.425 25.474 28.916 1.00 45.12 C ATOM 2946 O HIS B 203 27.212 25.595 28.950 1.00 43.27 O ATOM 2947 N PHE B 204 29.020 24.344 28.543 1.00 45.20 N ATOM 2948 CA PHE B 204 28.239 23.192 28.083 1.00 45.81 C ATOM 2949 CB PHE B 204 28.627 22.759 26.658 1.00 47.54 C ATOM 2950 CG PHE B 204 28.499 23.847 25.630 1.00 45.00 C ATOM 2951 CD1 PHE B 204 29.545 24.722 25.398 1.00 44.82 C ATOM 2952 CD2 PHE B 204 27.337 23.982 24.886 1.00 45.70 C ATOM 2953 CE1 PHE B 204 29.432 25.725 24.455 1.00 41.83 C ATOM 2954 CE2 PHE B 204 27.209 24.981 23.948 1.00 43.12 C ATOM 2955 CZ PHE B 204 28.257 25.850 23.726 1.00 44.90 C ATOM 2956 C PHE B 204 28.407 22.011 29.032 1.00 47.33 C ATOM 2957 O PHE B 204 29.522 21.679 29.423 1.00 44.83 O ATOM 2958 N ASP B 205 27.284 21.379 29.380 1.00 51.15 N ATOM 2959 CA ASP B 205 27.266 20.246 30.301 1.00 48.93 C ATOM 2960 CB ASP B 205 25.846 19.992 30.814 1.00 46.68 C ATOM 2961 CG ASP B 205 25.780 18.823 31.782 1.00 52.68 C ATOM 2962 OD1 ASP B 205 26.843 18.220 32.047 1.00 56.14 O ATOM 2963 OD2 ASP B 205 24.677 18.503 32.273 1.00 45.40 O ATOM 2964 C ASP B 205 27.842 18.977 29.677 1.00 47.80 C ATOM 2965 O ASP B 205 27.213 18.338 28.838 1.00 47.36 O ATOM 2966 N ASP B 206 29.043 18.613 30.112 1.00 49.84 N ATOM 2967 CA ASP B 206 29.750 17.453 29.577 1.00 48.20 C ATOM 2968 CB ASP B 206 31.237 17.513 29.926 1.00 52.08 C ATOM 2969 CG ASP B 206 32.109 16.763 28.923 1.00 57.14 C ATOM 2970 OD1 ASP B 206 31.648 16.509 27.784 1.00 55.43 O ATOM 2971 OD2 ASP B 206 33.259 16.432 29.279 1.00 54.06 O ATOM 2972 C ASP B 206 29.167 16.156 30.102 1.00 54.19 C ATOM 2973 O ASP B 206 29.698 15.082 29.822 1.00 54.08 O ATOM 2974 N ASP B 207 28.087 16.255 30.876 1.00 50.28 N ATOM 2975 CA ASP B 207 27.358 15.065 31.282 1.00 46.50 C ATOM 2976 CB ASP B 207 26.516 15.334 32.538 1.00 58.98 C ATOM 2977 CG ASP B 207 27.275 15.069 33.846 1.00 57.67 C ATOM 2978 OD1 ASP B 207 28.222 14.251 33.855 1.00 48.41 O ATOM 2979 OD2 ASP B 207 26.896 15.669 34.875 1.00 59.10 O ATOM 2980 C ASP B 207 26.482 14.524 30.129 1.00 48.55 C ATOM 2981 O ASP B 207 26.067 13.364 30.161 1.00 49.18 O ATOM 2982 N GLU B 208 26.200 15.357 29.122 1.00 48.01 N ATOM 2983 CA GLU B 208 25.488 14.890 27.923 1.00 49.23 C ATOM 2984 CB GLU B 208 24.781 16.035 27.183 1.00 42.52 C ATOM 2985 CG GLU B 208 24.146 17.075 28.092 1.00 50.85 C ATOM 2986 CD GLU B 208 23.093 16.485 29.027 1.00 47.96 C ATOM 2987 OE1 GLU B 208 22.586 15.371 28.765 1.00 40.85 O ATOM 2988 OE2 GLU B 208 22.777 17.143 30.029 1.00 46.06 O ATOM 2989 C GLU B 208 26.486 14.266 26.969 1.00 48.49 C ATOM 2990 O GLU B 208 27.631 14.692 26.915 1.00 53.58 O ATOM 2991 N LEU B 209 26.057 13.262 26.211 1.00 48.92 N ATOM 2992 CA LEU B 209 26.868 12.774 25.104 1.00 52.45 C ATOM 2993 CB LEU B 209 26.543 11.324 24.766 1.00 52.12 C ATOM 2994 CG LEU B 209 27.174 10.960 23.421 1.00 58.59 C ATOM 2995 CD1 LEU B 209 28.473 10.227 23.624 1.00 58.06 C ATOM 2996 CD2 LEU B 209 26.219 10.146 22.563 1.00 71.72 C ATOM 2997 C LEU B 209 26.641 13.663 23.876 1.00 53.15 C ATOM 2998 O LEU B 209 25.626 13.554 23.183 1.00 57.05 O ATOM 2999 N TRP B 210 27.584 14.557 23.615 1.00 51.07 N ATOM 3000 CA TRP B 210 27.410 15.534 22.553 1.00 49.23 C ATOM 3001 CB TRP B 210 28.338 16.723 22.783 1.00 46.32 C ATOM 3002 CG TRP B 210 27.880 17.521 23.929 1.00 45.08 C ATOM 3003 CD2 TRP B 210 26.733 18.374 23.965 1.00 45.20 C ATOM 3004 CE2 TRP B 210 26.654 18.912 25.263 1.00 47.09 C ATOM 3005 CE3 TRP B 210 25.762 18.733 23.023 1.00 46.54 C ATOM 3006 CD1 TRP B 210 28.437 17.569 25.172 1.00 48.35 C ATOM 3007 NE1 TRP B 210 27.709 18.411 25.982 1.00 49.39 N ATOM 3008 CZ2 TRP B 210 25.645 19.794 25.646 1.00 41.02 C ATOM 3009 CZ3 TRP B 210 24.761 19.615 23.406 1.00 45.27 C ATOM 3010 CH2 TRP B 210 24.718 20.137 24.709 1.00 41.16 C ATOM 3011 C TRP B 210 27.596 14.936 21.161 1.00 51.46 C ATOM 3012 O TRP B 210 28.537 14.174 20.922 1.00 51.60 O ATOM 3013 N SER B 211 26.686 15.296 20.257 1.00 48.38 N ATOM 3014 CA SER B 211 26.642 14.757 18.901 1.00 48.09 C ATOM 3015 CB SER B 211 25.478 13.769 18.749 1.00 57.94 C ATOM 3016 OG SER B 211 24.216 14.427 18.886 1.00 56.37 O ATOM 3017 C SER B 211 26.446 15.886 17.912 1.00 47.04 C ATOM 3018 O SER B 211 26.480 17.054 18.285 1.00 46.26 O ATOM 3019 N LEU B 212 26.237 15.524 16.647 1.00 58.09 N ATOM 3020 CA LEU B 212 25.923 16.489 15.594 1.00 53.43 C ATOM 3021 CB LEU B 212 27.140 16.772 14.722 1.00 48.82 C ATOM 3022 CG LEU B 212 28.111 17.821 15.255 1.00 49.32 C ATOM 3023 CD1 LEU B 212 29.260 18.066 14.271 1.00 40.74 C ATOM 3024 CD2 LEU B 212 27.346 19.093 15.523 1.00 41.76 C ATOM 3025 C LEU B 212 24.770 15.999 14.737 1.00 56.87 C ATOM 3026 O LEU B 212 24.091 16.794 14.082 1.00 59.66 O ATOM 3027 N GLY B 213 24.547 14.689 14.744 1.00 57.63 N ATOM 3028 CA GLY B 213 23.428 14.117 14.013 1.00 64.72 C ATOM 3029 C GLY B 213 22.146 14.079 14.828 1.00 62.18 C ATOM 3030 O GLY B 213 21.053 13.903 14.279 1.00 69.95 O ATOM 3031 O ALA B 393 24.996 17.016 21.345 1.00 20.00 O ATOM 3032 N ALA B 393 21.865 17.049 22.926 1.00 20.00 N ATOM 3033 CA ALA B 393 22.958 16.316 22.310 1.00 20.00 C ATOM 3034 C ALA B 393 23.810 17.096 21.301 1.00 20.00 C ATOM 3035 CB ALA B 393 22.453 15.051 21.688 1.00 20.00 C ATOM 3036 N SER B 394 23.208 17.837 20.405 1.00 31.84 N ATOM 3037 CA SER B 394 23.850 18.478 19.270 1.00 47.23 C ATOM 3038 CB SER B 394 22.868 18.746 18.133 1.00 38.96 C ATOM 3039 OG SER B 394 23.516 19.548 17.161 1.00 39.84 O ATOM 3040 C SER B 394 24.559 19.780 19.626 1.00 44.77 C ATOM 3041 O SER B 394 23.929 20.814 19.848 1.00 45.62 O ATOM 3042 N LEU B 395 25.879 19.739 19.614 1.00 38.86 N ATOM 3043 CA LEU B 395 26.653 20.863 20.103 1.00 44.28 C ATOM 3044 CB LEU B 395 28.132 20.475 20.156 1.00 46.21 C ATOM 3045 CG LEU B 395 29.184 21.460 20.651 1.00 45.64 C ATOM 3046 CD1 LEU B 395 28.938 21.911 22.114 1.00 46.28 C ATOM 3047 CD2 LEU B 395 30.550 20.815 20.493 1.00 43.54 C ATOM 3048 C LEU B 395 26.433 22.082 19.217 1.00 39.97 C ATOM 3049 O LEU B 395 26.518 23.218 19.664 1.00 45.54 O ATOM 3050 N PHE B 396 26.147 21.846 17.953 1.00 43.35 N ATOM 3051 CA PHE B 396 25.961 22.943 17.019 1.00 43.14 C ATOM 3052 CB PHE B 396 25.917 22.438 15.572 1.00 38.68 C ATOM 3053 CG PHE B 396 25.413 23.461 14.579 1.00 42.55 C ATOM 3054 CD1 PHE B 396 26.056 24.681 14.427 1.00 43.36 C ATOM 3055 CD2 PHE B 396 24.306 23.193 13.782 1.00 40.33 C ATOM 3056 CE1 PHE B 396 25.603 25.623 13.503 1.00 43.30 C ATOM 3057 CE2 PHE B 396 23.854 24.128 12.848 1.00 38.98 C ATOM 3058 CZ PHE B 396 24.501 25.344 12.711 1.00 36.50 C ATOM 3059 C PHE B 396 24.725 23.779 17.355 1.00 38.44 C ATOM 3060 O PHE B 396 24.822 24.998 17.412 1.00 38.76 O ATOM 3061 N LEU B 397 23.571 23.140 17.562 1.00 40.81 N ATOM 3062 CA LEU B 397 22.360 23.896 17.891 1.00 37.99 C ATOM 3063 CB LEU B 397 21.106 23.029 17.884 1.00 27.98 C ATOM 3064 CG LEU B 397 20.821 22.297 16.587 1.00 36.02 C ATOM 3065 CD1 LEU B 397 19.429 21.724 16.649 1.00 43.16 C ATOM 3066 CD2 LEU B 397 20.926 23.266 15.429 1.00 35.77 C ATOM 3067 C LEU B 397 22.547 24.524 19.263 1.00 41.97 C ATOM 3068 O LEU B 397 22.441 25.750 19.415 1.00 39.38 O ATOM 3069 N VAL B 398 22.835 23.693 20.261 1.00 34.24 N ATOM 3070 CA VAL B 398 22.992 24.227 21.602 1.00 42.00 C ATOM 3071 CB VAL B 398 23.555 23.188 22.621 1.00 42.68 C ATOM 3072 CG1 VAL B 398 23.606 23.798 23.991 1.00 37.54 C ATOM 3073 CG2 VAL B 398 22.715 21.926 22.647 1.00 37.57 C ATOM 3074 C VAL B 398 23.930 25.438 21.512 1.00 42.79 C ATOM 3075 O VAL B 398 23.595 26.519 22.005 1.00 46.44 O ATOM 3076 N ALA B 399 25.085 25.269 20.861 1.00 35.97 N ATOM 3077 CA ALA B 399 26.042 26.361 20.759 1.00 37.88 C ATOM 3078 CB ALA B 399 27.292 25.946 20.017 1.00 33.95 C ATOM 3079 C ALA B 399 25.397 27.591 20.132 1.00 42.15 C ATOM 3080 O ALA B 399 25.585 28.701 20.622 1.00 44.78 O ATOM 3081 N ALA B 400 24.599 27.393 19.081 1.00 43.05 N ATOM 3082 CA ALA B 400 23.942 28.516 18.391 1.00 46.31 C ATOM 3083 CB ALA B 400 23.166 28.027 17.145 1.00 43.26 C ATOM 3084 C ALA B 400 23.023 29.291 19.328 1.00 38.49 C ATOM 3085 O ALA B 400 23.013 30.517 19.342 1.00 38.90 O ATOM 3086 N HIS B 401 22.263 28.556 20.119 1.00 38.71 N ATOM 3087 CA HIS B 401 21.397 29.141 21.141 1.00 42.18 C ATOM 3088 CB HIS B 401 20.619 28.010 21.837 1.00 40.09 C ATOM 3089 CG HIS B 401 19.659 28.478 22.884 1.00 44.46 C ATOM 3090 CD2 HIS B 401 19.797 28.602 24.226 1.00 43.70 C ATOM 3091 ND1 HIS B 401 18.367 28.862 22.596 1.00 42.25 N ATOM 3092 CE1 HIS B 401 17.756 29.217 23.709 1.00 43.39 C ATOM 3093 NE2 HIS B 401 18.598 29.059 24.715 1.00 42.08 N ATOM 3094 C HIS B 401 22.194 29.963 22.168 1.00 43.24 C ATOM 3095 O HIS B 401 21.949 31.154 22.334 1.00 40.37 O ATOM 3096 N GLU B 402 23.154 29.321 22.842 1.00 40.98 N ATOM 3097 CA GLU B 402 23.927 29.965 23.908 1.00 40.21 C ATOM 3098 CB GLU B 402 24.857 28.944 24.576 1.00 39.33 C ATOM 3099 CG GLU B 402 24.118 27.762 25.172 1.00 45.42 C ATOM 3100 CD GLU B 402 23.089 28.209 26.220 1.00 49.45 C ATOM 3101 OE1 GLU B 402 22.063 27.508 26.400 1.00 39.99 O ATOM 3102 OE2 GLU B 402 23.310 29.275 26.849 1.00 44.58 O ATOM 3103 C GLU B 402 24.728 31.170 23.427 1.00 42.72 C ATOM 3104 O GLU B 402 24.994 32.104 24.191 1.00 39.03 O ATOM 3105 N PHE B 403 25.135 31.138 22.160 1.00 45.60 N ATOM 3106 CA PHE B 403 25.886 32.241 21.592 1.00 41.66 C ATOM 3107 CB PHE B 403 26.538 31.851 20.272 1.00 40.39 C ATOM 3108 CG PHE B 403 27.646 30.853 20.422 1.00 42.71 C ATOM 3109 CD1 PHE B 403 28.147 30.538 21.685 1.00 47.83 C ATOM 3110 CD2 PHE B 403 28.182 30.217 19.309 1.00 39.21 C ATOM 3111 CE1 PHE B 403 29.173 29.607 21.828 1.00 45.91 C ATOM 3112 CE2 PHE B 403 29.194 29.292 19.442 1.00 40.64 C ATOM 3113 CZ PHE B 403 29.692 28.981 20.694 1.00 41.55 C ATOM 3114 C PHE B 403 24.972 33.428 21.416 1.00 39.56 C ATOM 3115 O PHE B 403 25.416 34.562 21.457 1.00 48.69 O ATOM 3116 N GLY B 404 23.692 33.161 21.212 1.00 40.58 N ATOM 3117 CA GLY B 404 22.708 34.220 21.159 1.00 40.90 C ATOM 3118 C GLY B 404 22.736 34.926 22.503 1.00 44.38 C ATOM 3119 O GLY B 404 22.888 36.149 22.553 1.00 38.02 O ATOM 3120 N HIS B 405 22.594 34.151 23.585 1.00 43.52 N ATOM 3121 CA HIS B 405 22.738 34.682 24.954 1.00 46.34 C ATOM 3122 CB HIS B 405 22.736 33.563 26.013 1.00 37.18 C ATOM 3123 CG HIS B 405 21.388 32.948 26.273 1.00 45.70 C ATOM 3124 CD2 HIS B 405 21.040 31.699 26.672 1.00 43.87 C ATOM 3125 ND1 HIS B 405 20.203 33.650 26.169 1.00 46.58 N ATOM 3126 CE1 HIS B 405 19.189 32.855 26.462 1.00 45.43 C ATOM 3127 NE2 HIS B 405 19.672 31.672 26.790 1.00 41.46 N ATOM 3128 C HIS B 405 24.006 35.548 25.104 1.00 45.29 C ATOM 3129 O HIS B 405 23.912 36.726 25.475 1.00 42.28 O ATOM 3130 N ALA B 406 25.173 34.978 24.789 1.00 41.37 N ATOM 3131 CA ALA B 406 26.456 35.695 24.957 1.00 48.05 C ATOM 3132 CB ALA B 406 27.669 34.791 24.634 1.00 36.32 C ATOM 3133 C ALA B 406 26.502 36.983 24.135 1.00 47.12 C ATOM 3134 O ALA B 406 27.387 37.825 24.319 1.00 44.62 O ATOM 3135 N LEU B 407 25.534 37.134 23.236 1.00 42.62 N ATOM 3136 CA LEU B 407 25.402 38.371 22.475 1.00 44.73 C ATOM 3137 CB LEU B 407 24.996 38.076 21.034 1.00 41.36 C ATOM 3138 CG LEU B 407 25.989 37.166 20.320 1.00 41.66 C ATOM 3139 CD1 LEU B 407 25.588 37.075 18.887 1.00 39.67 C ATOM 3140 CD2 LEU B 407 27.423 37.686 20.465 1.00 34.07 C ATOM 3141 C LEU B 407 24.426 39.363 23.105 1.00 46.50 C ATOM 3142 O LEU B 407 24.402 40.523 22.709 1.00 50.58 O ATOM 3143 N GLY B 408 23.628 38.908 24.075 1.00 43.26 N ATOM 3144 CA GLY B 408 22.612 39.748 24.683 1.00 41.84 C ATOM 3145 C GLY B 408 21.173 39.389 24.315 1.00 45.91 C ATOM 3146 O GLY B 408 20.294 40.252 24.317 1.00 56.09 O ATOM 3147 N LEU B 409 20.916 38.127 23.995 1.00 40.40 N ATOM 3148 CA LEU B 409 19.546 37.701 23.722 1.00 43.87 C ATOM 3149 CB LEU B 409 19.440 36.882 22.435 1.00 45.76 C ATOM 3150 CG LEU B 409 19.584 37.591 21.090 1.00 42.11 C ATOM 3151 CD1 LEU B 409 19.261 36.606 20.003 1.00 40.96 C ATOM 3152 CD2 LEU B 409 18.659 38.778 21.007 1.00 37.92 C ATOM 3153 C LEU B 409 18.997 36.886 24.880 1.00 48.72 C ATOM 3154 O LEU B 409 19.710 36.084 25.489 1.00 45.21 O ATOM 3155 N ASP B 410 17.726 37.108 25.191 1.00 47.24 N ATOM 3156 CA ASP B 410 17.053 36.332 26.216 1.00 50.00 C ATOM 3157 CB ASP B 410 16.075 37.209 27.000 1.00 51.87 C ATOM 3158 CG ASP B 410 15.049 37.866 26.099 1.00 55.41 C ATOM 3159 OD1 ASP B 410 15.413 38.184 24.947 1.00 64.30 O ATOM 3160 OD2 ASP B 410 13.892 38.056 26.525 1.00 60.17 O ATOM 3161 C ASP B 410 16.284 35.274 25.471 1.00 46.23 C ATOM 3162 O ASP B 410 16.402 35.163 24.268 1.00 44.68 O ATOM 3163 N HIS B 411 15.475 34.506 26.180 1.00 49.05 N ATOM 3164 CA HIS B 411 14.694 33.487 25.509 1.00 48.46 C ATOM 3165 CB HIS B 411 14.170 32.472 26.516 1.00 43.18 C ATOM 3166 CG HIS B 411 15.195 31.459 26.911 1.00 44.42 C ATOM 3167 CD2 HIS B 411 15.960 30.636 26.157 1.00 44.83 C ATOM 3168 ND1 HIS B 411 15.559 31.229 28.219 1.00 45.44 N ATOM 3169 CE1 HIS B 411 16.485 30.289 28.253 1.00 47.86 C ATOM 3170 NE2 HIS B 411 16.741 29.911 27.015 1.00 49.24 N ATOM 3171 C HIS B 411 13.571 34.038 24.627 1.00 48.48 C ATOM 3172 O HIS B 411 13.070 35.155 24.840 1.00 47.25 O ATOM 3173 N SER B 412 13.210 33.248 23.621 1.00 40.03 N ATOM 3174 CA SER B 412 12.075 33.541 22.751 1.00 44.24 C ATOM 3175 CB SER B 412 12.431 33.227 21.298 1.00 38.75 C ATOM 3176 OG SER B 412 11.274 33.166 20.496 1.00 39.44 O ATOM 3177 C SER B 412 10.869 32.703 23.165 1.00 48.26 C ATOM 3178 O SER B 412 11.015 31.629 23.755 1.00 48.88 O ATOM 3179 N SER B 413 9.675 33.188 22.857 1.00 42.00 N ATOM 3180 CA SER B 413 8.478 32.426 23.161 1.00 44.46 C ATOM 3181 CB SER B 413 7.368 33.353 23.681 1.00 48.01 C ATOM 3182 OG SER B 413 7.259 34.529 22.882 1.00 44.41 O ATOM 3183 C SER B 413 8.029 31.681 21.914 1.00 49.55 C ATOM 3184 O SER B 413 7.130 30.839 21.956 1.00 48.99 O ATOM 3185 N VAL B 414 8.659 31.990 20.791 1.00 45.26 N ATOM 3186 CA VAL B 414 8.329 31.287 19.569 1.00 45.71 C ATOM 3187 CB VAL B 414 8.824 32.045 18.337 1.00 51.19 C ATOM 3188 CG1 VAL B 414 8.568 31.226 17.053 1.00 49.06 C ATOM 3189 CG2 VAL B 414 8.166 33.432 18.279 1.00 42.82 C ATOM 3190 C VAL B 414 8.969 29.920 19.649 1.00 47.17 C ATOM 3191 O VAL B 414 10.176 29.819 19.785 1.00 51.35 O ATOM 3192 N PRO B 415 8.157 28.859 19.582 1.00 50.00 N ATOM 3193 CD PRO B 415 6.687 28.881 19.566 1.00 49.27 C ATOM 3194 CA PRO B 415 8.679 27.506 19.775 1.00 48.38 C ATOM 3195 CB PRO B 415 7.413 26.639 19.837 1.00 51.16 C ATOM 3196 CG PRO B 415 6.332 27.578 20.220 1.00 47.43 C ATOM 3197 C PRO B 415 9.620 27.018 18.684 1.00 44.25 C ATOM 3198 O PRO B 415 10.433 26.152 18.981 1.00 50.46 O ATOM 3199 N GLU B 416 9.538 27.527 17.461 1.00 45.10 N ATOM 3200 CA GLU B 416 10.539 27.120 16.457 1.00 46.77 C ATOM 3201 CB GLU B 416 9.943 26.908 15.058 1.00 46.78 C ATOM 3202 CG GLU B 416 8.798 27.853 14.704 1.00 55.40 C ATOM 3203 CD GLU B 416 7.559 27.549 15.518 1.00 48.72 C ATOM 3204 OE1 GLU B 416 6.909 26.526 15.218 1.00 45.88 O ATOM 3205 OE2 GLU B 416 7.260 28.311 16.469 1.00 49.92 O ATOM 3206 C GLU B 416 11.727 28.076 16.406 1.00 46.88 C ATOM 3207 O GLU B 416 12.694 27.837 15.675 1.00 42.65 O ATOM 3208 N ALA B 417 11.646 29.151 17.188 1.00 46.36 N ATOM 3209 CA ALA B 417 12.739 30.104 17.272 1.00 46.27 C ATOM 3210 CB ALA B 417 12.369 31.286 18.147 1.00 41.55 C ATOM 3211 C ALA B 417 13.918 29.364 17.853 1.00 44.35 C ATOM 3212 O ALA B 417 13.740 28.414 18.609 1.00 48.38 O ATOM 3213 N LEU B 418 15.116 29.779 17.466 1.00 42.10 N ATOM 3214 CA LEU B 418 16.360 29.189 17.950 1.00 42.90 C ATOM 3215 CB LEU B 418 17.502 29.705 17.082 1.00 34.00 C ATOM 3216 CG LEU B 418 18.965 29.371 17.371 1.00 38.38 C ATOM 3217 CD1 LEU B 418 19.619 30.489 18.140 1.00 44.49 C ATOM 3218 CD2 LEU B 418 19.098 28.066 18.100 1.00 34.02 C ATOM 3219 C LEU B 418 16.592 29.513 19.446 1.00 43.30 C ATOM 3220 O LEU B 418 17.064 28.664 20.238 1.00 30.24 O ATOM 3221 N MET B 419 16.232 30.744 19.815 1.00 40.37 N ATOM 3222 CA MET B 419 16.341 31.202 21.195 1.00 43.13 C ATOM 3223 CB MET B 419 16.431 32.727 21.259 1.00 38.00 C ATOM 3224 CG MET B 419 17.714 33.273 20.708 1.00 38.59 C ATOM 3225 SD MET B 419 19.140 32.362 21.329 1.00 36.55 S ATOM 3226 CE MET B 419 19.069 32.721 23.068 1.00 43.44 C ATOM 3227 C MET B 419 15.206 30.700 22.103 1.00 40.77 C ATOM 3228 O MET B 419 15.089 31.150 23.231 1.00 37.22 O ATOM 3229 N TYR B 420 14.380 29.790 21.593 1.00 41.96 N ATOM 3230 CA TYR B 420 13.399 29.078 22.387 1.00 38.40 C ATOM 3231 CB TYR B 420 12.582 28.191 21.473 1.00 38.92 C ATOM 3232 CG TYR B 420 11.326 27.615 22.096 1.00 48.58 C ATOM 3233 CD1 TYR B 420 10.290 28.445 22.530 1.00 46.36 C ATOM 3234 CE1 TYR B 420 9.135 27.912 23.081 1.00 50.31 C ATOM 3235 CD2 TYR B 420 11.163 26.240 22.232 1.00 49.49 C ATOM 3236 CE2 TYR B 420 10.014 25.703 22.786 1.00 49.34 C ATOM 3237 CZ TYR B 420 9.000 26.541 23.204 1.00 49.93 C ATOM 3238 OH TYR B 420 7.860 26.000 23.758 1.00 48.40 O ATOM 3239 C TYR B 420 14.185 28.204 23.344 1.00 43.10 C ATOM 3240 O TYR B 420 15.200 27.670 22.953 1.00 50.34 O ATOM 3241 N PRO B 421 13.724 28.045 24.599 1.00 46.87 N ATOM 3242 CD PRO B 421 12.437 28.533 25.123 1.00 43.66 C ATOM 3243 CA PRO B 421 14.513 27.351 25.632 1.00 43.05 C ATOM 3244 CB PRO B 421 13.757 27.656 26.932 1.00 46.49 C ATOM 3245 CG PRO B 421 12.702 28.659 26.585 1.00 46.73 C ATOM 3246 C PRO B 421 14.589 25.836 25.474 1.00 43.96 C ATOM 3247 O PRO B 421 15.599 25.259 25.857 1.00 50.96 O ATOM 3248 N MET B 422 13.542 25.195 24.969 1.00 45.92 N ATOM 3249 CA MET B 422 13.508 23.735 24.919 1.00 46.43 C ATOM 3250 CB MET B 422 12.085 23.200 24.727 1.00 48.11 C ATOM 3251 CG MET B 422 11.087 23.629 25.767 1.00 54.78 C ATOM 3252 SD MET B 422 9.704 22.487 25.780 1.00 60.93 S ATOM 3253 CE MET B 422 8.919 22.903 24.226 1.00 59.18 C ATOM 3254 C MET B 422 14.329 23.255 23.758 1.00 46.56 C ATOM 3255 O MET B 422 14.221 23.786 22.653 1.00 51.73 O ATOM 3256 N TYR B 423 15.141 22.234 23.995 1.00 50.18 N ATOM 3257 CA TYR B 423 15.897 21.631 22.904 1.00 54.16 C ATOM 3258 CB TYR B 423 16.888 20.583 23.422 1.00 50.11 C ATOM 3259 CG TYR B 423 17.673 19.867 22.344 1.00 47.38 C ATOM 3260 CD1 TYR B 423 17.280 18.625 21.882 1.00 45.37 C ATOM 3261 CE1 TYR B 423 18.001 17.959 20.908 1.00 43.64 C ATOM 3262 CD2 TYR B 423 18.820 20.431 21.801 1.00 52.51 C ATOM 3263 CE2 TYR B 423 19.549 19.779 20.810 1.00 47.48 C ATOM 3264 CZ TYR B 423 19.137 18.543 20.367 1.00 48.38 C ATOM 3265 OH TYR B 423 19.860 17.886 19.385 1.00 43.16 O ATOM 3266 C TYR B 423 14.925 21.005 21.916 1.00 55.79 C ATOM 3267 O TYR B 423 13.899 20.426 22.298 1.00 56.90 O ATOM 3268 N ARG B 424 15.236 21.154 20.640 1.00 54.64 N ATOM 3269 CA ARG B 424 14.504 20.460 19.597 1.00 55.63 C ATOM 3270 CB ARG B 424 13.189 21.168 19.282 1.00 60.69 C ATOM 3271 CG ARG B 424 12.322 20.424 18.275 1.00 70.01 C ATOM 3272 CD ARG B 424 10.905 20.180 18.814 1.00 84.40 C ATOM 3273 NE ARG B 424 10.117 21.413 18.927 1.00 90.01 N ATOM 3274 CZ ARG B 424 9.580 21.879 20.056 1.00 85.20 C ATOM 3275 NH1 ARG B 424 9.728 21.216 21.205 1.00 73.44 N ATOM 3276 NH2 ARG B 424 8.882 23.013 20.035 1.00 74.32 N ATOM 3277 C ARG B 424 15.406 20.449 18.390 1.00 53.00 C ATOM 3278 O ARG B 424 15.883 21.497 17.959 1.00 57.35 O ATOM 3279 N PHE B 425 15.651 19.268 17.846 1.00 53.36 N ATOM 3280 CA PHE B 425 16.571 19.132 16.726 1.00 55.20 C ATOM 3281 CB PHE B 425 17.329 17.811 16.871 1.00 52.73 C ATOM 3282 CG PHE B 425 18.105 17.417 15.663 1.00 52.30 C ATOM 3283 CD1 PHE B 425 19.334 17.983 15.398 1.00 57.98 C ATOM 3284 CD2 PHE B 425 17.610 16.463 14.792 1.00 58.13 C ATOM 3285 CE1 PHE B 425 20.061 17.602 14.273 1.00 61.84 C ATOM 3286 CE2 PHE B 425 18.326 16.080 13.672 1.00 59.12 C ATOM 3287 CZ PHE B 425 19.555 16.652 13.409 1.00 57.97 C ATOM 3288 C PHE B 425 15.886 19.196 15.363 1.00 56.78 C ATOM 3289 O PHE B 425 15.056 18.349 15.061 1.00 61.00 O ATOM 3290 N THR B 426 16.235 20.195 14.545 1.00 60.79 N ATOM 3291 CA THR B 426 15.917 20.173 13.102 1.00 58.67 C ATOM 3292 CB THR B 426 15.086 21.390 12.628 1.00 59.11 C ATOM 3293 OG1 THR B 426 15.684 22.600 13.121 1.00 52.73 O ATOM 3294 CG2 THR B 426 13.626 21.283 13.088 1.00 61.58 C ATOM 3295 C THR B 426 17.162 20.153 12.221 1.00 57.12 C ATOM 3296 O THR B 426 18.278 20.392 12.684 1.00 58.59 O ATOM 3297 N GLU B 427 16.957 19.878 10.936 1.00 61.70 N ATOM 3298 CA GLU B 427 18.023 19.989 9.952 1.00 60.13 C ATOM 3299 CB GLU B 427 17.931 18.868 8.908 1.00 54.67 C ATOM 3300 CG GLU B 427 17.960 17.470 9.518 1.00 65.42 C ATOM 3301 CD GLU B 427 18.893 16.515 8.781 1.00 72.62 C ATOM 3302 OE1 GLU B 427 19.179 15.422 9.330 1.00 60.84 O ATOM 3303 OE2 GLU B 427 19.338 16.859 7.659 1.00 73.29 O ATOM 3304 C GLU B 427 17.907 21.348 9.282 1.00 54.90 C ATOM 3305 O GLU B 427 18.825 21.782 8.585 1.00 45.97 O ATOM 3306 N GLY B 428 16.768 22.009 9.512 1.00 48.91 N ATOM 3307 CA GLY B 428 16.473 23.309 8.921 1.00 44.87 C ATOM 3308 C GLY B 428 17.435 24.395 9.366 1.00 46.25 C ATOM 3309 O GLY B 428 18.184 24.198 10.308 1.00 50.84 O ATOM 3310 N PRO B 429 17.439 25.546 8.676 1.00 49.06 N ATOM 3311 CD PRO B 429 16.787 25.806 7.384 1.00 41.83 C ATOM 3312 CA PRO B 429 18.223 26.699 9.132 1.00 44.60 C ATOM 3313 CB PRO B 429 17.846 27.781 8.124 1.00 42.97 C ATOM 3314 CG PRO B 429 17.441 27.049 6.925 1.00 38.99 C ATOM 3315 C PRO B 429 17.783 27.125 10.532 1.00 44.35 C ATOM 3316 O PRO B 429 16.614 27.448 10.734 1.00 47.95 O ATOM 3317 N PRO B 430 18.713 27.144 11.491 1.00 41.86 N ATOM 3318 CD PRO B 430 20.157 26.970 11.267 1.00 31.48 C ATOM 3319 CA PRO B 430 18.360 27.334 12.914 1.00 36.00 C ATOM 3320 CB PRO B 430 19.710 27.239 13.636 1.00 37.66 C ATOM 3321 CG PRO B 430 20.653 26.555 12.625 1.00 45.83 C ATOM 3322 C PRO B 430 17.688 28.677 13.221 1.00 35.43 C ATOM 3323 O PRO B 430 16.840 28.739 14.105 1.00 38.65 O ATOM 3324 N LEU B 431 18.052 29.734 12.502 1.00 31.04 N ATOM 3325 CA LEU B 431 17.486 31.060 12.746 1.00 35.74 C ATOM 3326 CB LEU B 431 18.314 32.139 12.058 1.00 25.12 C ATOM 3327 CG LEU B 431 19.736 32.394 12.542 1.00 33.35 C ATOM 3328 CD1 LEU B 431 20.207 33.681 11.914 1.00 30.44 C ATOM 3329 CD2 LEU B 431 19.862 32.454 14.072 1.00 35.88 C ATOM 3330 C LEU B 431 16.001 31.212 12.324 1.00 47.91 C ATOM 3331 O LEU B 431 15.603 30.832 11.210 1.00 39.81 O ATOM 3332 N HIS B 432 15.182 31.787 13.201 1.00 41.39 N ATOM 3333 CA HIS B 432 13.831 32.154 12.774 1.00 48.82 C ATOM 3334 CB HIS B 432 12.778 31.465 13.648 1.00 47.68 C ATOM 3335 CG HIS B 432 11.448 31.296 12.981 1.00 56.60 C ATOM 3336 CD2 HIS B 432 10.241 31.866 13.232 1.00 52.63 C ATOM 3337 ND1 HIS B 432 11.250 30.433 11.922 1.00 60.75 N ATOM 3338 CE1 HIS B 432 9.984 30.490 11.541 1.00 62.14 C ATOM 3339 NE2 HIS B 432 9.352 31.352 12.319 1.00 53.00 N ATOM 3340 C HIS B 432 13.674 33.681 12.792 1.00 48.04 C ATOM 3341 O HIS B 432 14.528 34.388 13.330 1.00 42.82 O ATOM 3342 N LYS B 433 12.608 34.193 12.187 1.00 47.13 N ATOM 3343 CA LYS B 433 12.342 35.625 12.268 1.00 46.56 C ATOM 3344 CB LYS B 433 10.928 35.939 11.766 1.00 47.48 C ATOM 3345 CG LYS B 433 10.780 35.966 10.220 1.00 49.30 C ATOM 3346 CD LYS B 433 9.336 35.717 9.799 1.00 51.05 C ATOM 3347 CE LYS B 433 9.177 35.601 8.280 1.00 44.20 C ATOM 3348 NZ LYS B 433 9.195 36.933 7.641 1.00 45.78 N ATOM 3349 C LYS B 433 12.567 36.192 13.685 1.00 41.72 C ATOM 3350 O LYS B 433 13.198 37.228 13.859 1.00 40.57 O ATOM 3351 N ASP B 434 12.067 35.515 14.708 1.00 41.39 N ATOM 3352 CA ASP B 434 12.199 36.063 16.056 1.00 41.15 C ATOM 3353 CB ASP B 434 11.412 35.224 17.055 1.00 45.00 C ATOM 3354 CG ASP B 434 11.112 35.984 18.340 1.00 44.21 C ATOM 3355 OD1 ASP B 434 10.663 37.145 18.249 1.00 45.43 O ATOM 3356 OD2 ASP B 434 11.316 35.415 19.435 1.00 42.52 O ATOM 3357 C ASP B 434 13.652 36.235 16.554 1.00 43.60 C ATOM 3358 O ASP B 434 13.956 37.172 17.322 1.00 41.61 O ATOM 3359 N ASP B 435 14.541 35.329 16.153 1.00 34.70 N ATOM 3360 CA ASP B 435 15.917 35.405 16.612 1.00 37.69 C ATOM 3361 CB ASP B 435 16.635 34.079 16.428 1.00 36.39 C ATOM 3362 CG ASP B 435 15.807 32.904 16.885 1.00 41.20 C ATOM 3363 OD1 ASP B 435 15.189 32.984 17.970 1.00 39.14 O ATOM 3364 OD2 ASP B 435 15.778 31.895 16.147 1.00 43.08 O ATOM 3365 C ASP B 435 16.640 36.531 15.879 1.00 38.55 C ATOM 3366 O ASP B 435 17.540 37.159 16.423 1.00 38.68 O ATOM 3367 N VAL B 436 16.213 36.802 14.654 1.00 37.46 N ATOM 3368 CA VAL B 436 16.787 37.881 13.869 1.00 44.09 C ATOM 3369 CB VAL B 436 16.510 37.686 12.370 1.00 39.41 C ATOM 3370 CG1 VAL B 436 17.004 38.893 11.581 1.00 42.07 C ATOM 3371 CG2 VAL B 436 17.172 36.430 11.897 1.00 40.53 C ATOM 3372 C VAL B 436 16.285 39.252 14.343 1.00 44.98 C ATOM 3373 O VAL B 436 17.082 40.118 14.743 1.00 45.81 O ATOM 3374 N ASN B 437 14.969 39.440 14.286 1.00 35.29 N ATOM 3375 CA ASN B 437 14.342 40.612 14.872 1.00 40.68 C ATOM 3376 CB ASN B 437 12.861 40.344 15.128 1.00 40.62 C ATOM 3377 CG ASN B 437 12.078 40.078 13.853 1.00 39.74 C ATOM 3378 OD1 ASN B 437 12.501 40.421 12.738 1.00 36.67 O ATOM 3379 ND2 ASN B 437 10.914 39.469 14.015 1.00 47.43 N ATOM 3380 C ASN B 437 14.995 40.968 16.195 1.00 40.69 C ATOM 3381 O ASN B 437 15.279 42.129 16.462 1.00 43.71 O ATOM 3382 N GLY B 438 15.234 39.952 17.018 1.00 40.21 N ATOM 3383 CA GLY B 438 15.805 40.160 18.335 1.00 47.05 C ATOM 3384 C GLY B 438 17.207 40.719 18.243 1.00 45.13 C ATOM 3385 O GLY B 438 17.489 41.827 18.706 1.00 46.59 O ATOM 3386 N ILE B 439 18.099 39.962 17.620 1.00 47.04 N ATOM 3387 CA ILE B 439 19.467 40.444 17.473 1.00 47.91 C ATOM 3388 CB ILE B 439 20.350 39.501 16.644 1.00 41.16 C ATOM 3389 CG2 ILE B 439 19.998 39.575 15.133 1.00 38.05 C ATOM 3390 CG1 ILE B 439 21.822 39.809 16.932 1.00 41.14 C ATOM 3391 CD1 ILE B 439 22.212 39.533 18.344 1.00 41.71 C ATOM 3392 C ILE B 439 19.506 41.851 16.884 1.00 45.15 C ATOM 3393 O ILE B 439 20.248 42.700 17.371 1.00 47.07 O ATOM 3394 N ARG B 440 18.690 42.106 15.866 1.00 39.41 N ATOM 3395 CA ARG B 440 18.785 43.373 15.162 1.00 43.98 C ATOM 3396 CB ARG B 440 17.818 43.437 13.983 1.00 50.48 C ATOM 3397 CG ARG B 440 18.290 42.715 12.723 1.00 51.65 C ATOM 3398 CD ARG B 440 17.251 42.829 11.605 1.00 41.78 C ATOM 3399 NE ARG B 440 17.611 42.024 10.450 1.00 52.28 N ATOM 3400 CZ ARG B 440 16.880 41.922 9.345 1.00 57.86 C ATOM 3401 NH1 ARG B 440 15.726 42.571 9.256 1.00 54.34 N ATOM 3402 NH2 ARG B 440 17.299 41.161 8.332 1.00 49.06 N ATOM 3403 C ARG B 440 18.503 44.489 16.142 1.00 51.17 C ATOM 3404 O ARG B 440 19.185 45.513 16.147 1.00 52.09 O ATOM 3405 N HIS B 441 17.503 44.275 16.987 1.00 44.90 N ATOM 3406 CA HIS B 441 17.167 45.241 18.012 1.00 47.41 C ATOM 3407 CB HIS B 441 16.132 44.637 18.953 1.00 48.60 C ATOM 3408 CG HIS B 441 15.343 45.651 19.707 1.00 55.13 C ATOM 3409 CD2 HIS B 441 14.392 46.522 19.299 1.00 59.97 C ATOM 3410 ND1 HIS B 441 15.507 45.864 21.060 1.00 60.72 N ATOM 3411 CE1 HIS B 441 14.685 46.822 21.455 1.00 64.18 C ATOM 3412 NE2 HIS B 441 13.998 47.239 20.406 1.00 71.86 N ATOM 3413 C HIS B 441 18.426 45.674 18.777 1.00 53.33 C ATOM 3414 O HIS B 441 18.737 46.861 18.857 1.00 56.08 O ATOM 3415 N LEU B 442 19.161 44.713 19.325 1.00 49.59 N ATOM 3416 CA LEU B 442 20.456 45.006 19.938 1.00 52.14 C ATOM 3417 CB LEU B 442 21.174 43.710 20.341 1.00 46.62 C ATOM 3418 CG LEU B 442 20.827 43.058 21.678 1.00 55.43 C ATOM 3419 CD1 LEU B 442 21.036 44.068 22.819 1.00 64.79 C ATOM 3420 CD2 LEU B 442 19.408 42.501 21.688 1.00 45.82 C ATOM 3421 C LEU B 442 21.388 45.818 19.028 1.00 50.90 C ATOM 3422 O LEU B 442 21.899 46.868 19.421 1.00 47.83 O ATOM 3423 N TYR B 443 21.630 45.299 17.825 1.00 51.71 N ATOM 3424 CA TYR B 443 22.635 45.857 16.921 1.00 52.80 C ATOM 3425 CB TYR B 443 23.758 44.838 16.677 1.00 51.98 C ATOM 3426 CG TYR B 443 24.266 44.166 17.945 1.00 49.74 C ATOM 3427 CD1 TYR B 443 23.865 42.880 18.289 1.00 48.37 C ATOM 3428 CE1 TYR B 443 24.311 42.273 19.444 1.00 49.63 C ATOM 3429 CD2 TYR B 443 25.135 44.828 18.801 1.00 51.18 C ATOM 3430 CE2 TYR B 443 25.596 44.232 19.963 1.00 47.29 C ATOM 3431 CZ TYR B 443 25.182 42.957 20.284 1.00 54.49 C ATOM 3432 OH TYR B 443 25.646 42.368 21.447 1.00 44.92 O ATOM 3433 C TYR B 443 21.989 46.287 15.599 1.00 49.23 C ATOM 3434 O TYR B 443 21.958 47.463 15.270 1.00 43.95 O ATOM 3435 N GLY B 444 21.472 45.320 14.849 1.00 59.32 N ATOM 3436 CA GLY B 444 20.739 45.603 13.623 1.00 60.84 C ATOM 3437 C GLY B 444 21.490 46.439 12.613 1.00 59.87 C ATOM 3438 O GLY B 444 21.628 46.042 11.453 1.00 75.23 O ATOM 3439 ZN ZN B 500 18.838 29.756 26.785 1.00 46.43 Zn ATOM 3440 ZN ZN B 501 28.420 27.416 34.020 1.00 49.83 Zn ATOM 3441 CA CA B 502 22.047 17.943 32.177 1.00 60.92 Ca ATOM 3442 CA CA B 503 29.961 13.344 27.676 1.00 68.05 Ca ATOM 3443 CA CA B 504 33.455 36.117 29.287 1.00 61.68 Ca TER 3444 CA B 504 ATOM 3501 C01 LIG E 1 19.271 43.772 −8.671 1.00 47.08 A C ATOM 3502 C02 LIG E 1 19.125 43.041 −9.954 1.00 55.16 A C ATOM 3503 N03 LIG E 1 19.227 43.463 −11.173 1.00 46.06 A N ATOM 3504 C04 LIG E 1 19.006 42.397 −12.061 1.00 46.95 A C ATOM 3505 C05 LIG E 1 19.051 42.805 −13.482 1.00 49.25 A C ATOM 3506 C06 LIG E 1 18.751 41.159 −11.521 1.00 51.62 A C ATOM 3507 S07 LIG E 1 18.813 41.325 −9.809 1.00 50.76 A S ATOM 3508 C08 LIG E 1 18.596 39.749 −11.958 1.00 49.69 A C ATOM 3509 C09 LIG E 1 18.343 38.792 −11.051 1.00 49.91 A C ATOM 3510 S10 LIG E 1 18.203 37.229 −11.675 1.00 47.36 A S ATOM 3511 C11 LIG E 1 18.499 37.889 −13.253 1.00 43.92 A C ATOM 3512 N12 LIG E 1 18.694 39.181 −13.267 1.00 47.32 A N ATOM 3513 N13 LIG E 1 18.528 37.033 −14.359 1.00 44.50 A N ATOM 3514 C14 LIG E 1 18.937 37.239 −15.723 1.00 47.19 A C ATOM 3515 C15 LIG E 1 19.503 38.461 −16.082 1.00 47.31 A C ATOM 3516 C16 LIG E 1 19.872 38.953 −17.346 1.00 48.74 A C ATOM 3517 C17 LIG E 1 19.651 38.008 −18.316 1.00 43.63 A C ATOM 3518 C18 LIG E 1 19.032 36.799 −18.035 1.00 44.86 A C ATOM 3519 C19 LIG E 1 18.670 36.343 −16.771 1.00 45.50 A C ATOM 3520 O20 LIG E 1 18.067 35.183 −16.456 1.00 46.15 A O ATOM 3521 C21 LIG E 1 18.197 33.971 −17.142 1.00 43.46 A C ATOM 3522 C22 LIG E 1 17.477 32.902 −16.359 1.00 42.00 A C ATOM 3523 C23 LIG E 1 19.668 33.631 −17.068 1.00 41.39 A C ATOM 3524 S24 LIG E 1 20.461 40.559 −17.600 1.00 47.47 A S ATOM 3525 N25 LIG E 1 22.012 40.809 −17.441 1.00 58.41 A N ATOM 3526 O26 LIG E 1 20.251 40.881 −18.886 1.00 55.02 A O ATOM 3527 O27 LIG E 1 19.967 41.339 −16.632 1.00 51.32 A O TER 3528 LIG E 1 END ATOM 1 N THR A 40 3.580 62.492 27.428 1.00 62.75 A N ATOM 2 CA THR A 40 4.940 62.991 27.307 1.00 58.36 A C ATOM 3 C THR A 40 5.117 63.876 26.067 1.00 54.85 A C ATOM 4 CB THR A 40 5.976 61.829 27.293 1.00 57.75 A C ATOM 5 OG1 THR A 40 7.258 62.302 27.739 1.00 54.58 A O ATOM 6 CG2 THR A 40 6.092 61.207 25.896 1.00 48.26 A C ATOM 7 O THR A 40 6.225 64.327 25.793 1.00 55.72 A O ATOM 8 CB ASP A 41 2.809 65.010 23.347 1.00 40.17 A C ATOM 9 CG ASP A 41 2.532 63.689 22.660 1.00 41.78 A C ATOM 10 OD1 ASP A 41 3.353 62.761 22.802 1.00 49.03 A O ATOM 11 OD2 ASP A 41 1.490 63.570 21.983 1.00 39.34 A O ATOM 12 C ASP A 41 4.533 66.425 24.492 1.00 47.53 A C ATOM 13 O ASP A 41 5.320 67.049 23.783 1.00 49.17 A O ATOM 14 N ASP A 41 4.038 64.133 25.323 1.00 49.77 A N ATOM 15 CA ASP A 41 4.121 64.998 24.137 1.00 48.30 A C ATOM 16 N ARG A 42 3.998 66.946 25.586 1.00 49.44 A N ATOM 17 CA ARG A 42 4.430 68.236 26.098 1.00 46.62 A C ATOM 18 CB ARG A 42 3.592 68.603 27.323 1.00 52.31 A C ATOM 19 CG ARG A 42 4.021 69.855 28.074 1.00 57.05 A C ATOM 20 CD ARG A 42 3.298 71.093 27.579 1.00 54.75 A C ATOM 21 NE ARG A 42 3.613 72.270 28.393 1.00 56.94 A N ATOM 22 CZ ARG A 42 2.899 73.395 28.385 1.00 57.02 A C ATOM 23 NH1 ARG A 42 1.818 73.499 27.613 1.00 49.33 A N ATOM 24 NH2 ARG A 42 3.266 74.418 29.146 1.00 59.81 A N ATOM 25 C ARG A 42 5.924 68.158 26.444 1.00 49.20 A C ATOM 26 O ARG A 42 6.665 69.111 26.228 1.00 48.84 A O ATOM 27 N GLN A 43 6.345 67.010 26.977 1.00 52.77 A N ATOM 28 CA GLN A 43 7.743 66.720 27.320 1.00 47.89 A C ATOM 29 CB GLN A 43 7.868 65.301 27.896 1.00 52.21 A C ATOM 30 CG GLN A 43 7.332 65.068 29.329 1.00 64.15 A C ATOM 31 CD GLN A 43 5.929 65.615 29.560 1.00 63.97 A C ATOM 32 OE1 GLN A 43 4.951 65.191 28.916 1.00 60.46 A O ATOM 33 NE2 GLN A 43 5.820 66.557 30.498 1.00 67.30 A N ATOM 34 C GLN A 43 8.624 66.761 26.083 1.00 47.32 A C ATOM 35 O GLN A 43 9.743 67.262 26.111 1.00 43.62 A O ATOM 36 N LEU A 44 8.118 66.168 25.014 1.00 41.39 A N ATOM 37 CA LEU A 44 8.855 66.028 23.782 1.00 45.22 A C ATOM 38 CB LEU A 44 8.022 65.249 22.779 1.00 43.61 A C ATOM 39 CG LEU A 44 8.776 64.795 21.542 1.00 40.21 A C ATOM 40 CD1 LEU A 44 9.571 63.566 21.925 1.00 49.88 A C ATOM 41 CD2 LEU A 44 7.831 64.470 20.424 1.00 38.41 A C ATOM 42 C LEU A 44 9.135 67.403 23.219 1.00 41.41 A C ATOM 43 O LEU A 44 10.260 67.725 22.885 1.00 40.18 A O ATOM 44 N ALA A 45 8.085 68.203 23.137 1.00 35.34 A N ATOM 45 CA ALA A 45 8.145 69.529 22.572 1.00 33.60 A C ATOM 46 CB ALA A 45 6.725 70.126 22.450 1.00 38.71 A C ATOM 47 C ALA A 45 9.040 70.463 23.364 1.00 38.36 A C ATOM 48 O ALA A 45 9.706 71.328 22.792 1.00 38.44 A O ATOM 49 N GLU A 46 9.042 70.317 24.681 1.00 39.71 A N ATOM 50 CA GLU A 46 9.845 71.200 25.491 1.00 42.03 A C ATOM 51 CB GLU A 46 9.537 71.007 26.974 1.00 43.99 A C ATOM 52 CG GLU A 46 8.257 71.725 27.410 1.00 54.77 A C ATOM 53 CD GLU A 46 7.667 71.195 28.726 1.00 65.94 A C ATOM 54 OE1 GLU A 46 8.373 70.476 29.476 1.00 65.43 A O ATOM 55 OE2 GLU A 46 6.485 71.507 29.007 1.00 62.78 A O ATOM 56 C GLU A 46 11.317 70.953 25.199 1.00 40.40 A C ATOM 57 O GLU A 46 12.103 71.896 25.048 1.00 40.18 A O ATOM 58 N GLU A 47 11.676 69.676 25.121 1.00 39.60 A N ATOM 59 CA GLU A 47 13.061 69.268 24.917 1.00 42.86 A C ATOM 60 CB GLU A 47 13.202 67.769 25.178 1.00 44.76 A C ATOM 61 CG GLU A 47 13.992 67.017 24.135 1.00 52.11 A C ATOM 62 CD GLU A 47 15.436 66.789 24.537 1.00 63.02 A C ATOM 63 OE1 GLU A 47 15.692 66.620 25.756 1.00 63.91 A O ATOM 64 OE2 GLU A 47 16.304 66.765 23.628 1.00 51.14 A O ATOM 65 C GLU A 47 13.553 69.654 23.513 1.00 41.05 A C ATOM 66 O GLU A 47 14.655 70.174 23.353 1.00 41.88 A O ATOM 67 N TYR A 48 12.721 69.421 22.506 1.00 38.79 A N ATOM 68 CA TYR A 48 13.006 69.881 21.158 1.00 35.96 A C ATOM 69 CB TYR A 48 11.845 69.506 20.270 1.00 31.64 A C ATOM 70 CG TYR A 48 12.081 69.533 18.791 1.00 28.89 A C ATOM 71 CD1 TYR A 48 12.041 70.726 18.086 1.00 30.84 A C ATOM 72 CE1 TYR A 48 12.225 70.750 16.719 1.00 27.12 A C ATOM 73 CD2 TYR A 48 12.285 68.355 18.080 1.00 31.64 A C ATOM 74 CE2 TYR A 48 12.467 68.365 16.710 1.00 26.48 A C ATOM 75 CZ TYR A 48 12.449 69.569 16.041 1.00 28.04 A C ATOM 76 OH TYR A 48 12.619 69.589 14.680 1.00 23.38 A O ATOM 77 C TYR A 48 13.188 71.396 21.159 1.00 39.41 A C ATOM 78 O TYR A 48 14.231 71.899 20.751 1.00 36.31 A O ATOM 79 N LEU A 49 12.183 72.134 21.616 1.00 35.31 A N ATOM 80 CA LEU A 49 12.272 73.587 21.580 1.00 36.48 A C ATOM 81 CB LEU A 49 11.069 74.221 22.273 1.00 33.93 A C ATOM 82 CG LEU A 49 9.792 74.029 21.473 1.00 37.32 A C ATOM 83 CD1 LEU A 49 8.613 74.395 22.353 1.00 33.67 A C ATOM 84 CD2 LEU A 49 9.804 74.825 20.165 1.00 33.93 A C ATOM 85 C LEU A 49 13.540 74.084 22.239 1.00 33.29 A C ATOM 86 O LEU A 49 14.088 75.115 21.869 1.00 35.00 A O ATOM 87 N TYR A 50 13.990 73.376 23.254 1.00 32.59 A N ATOM 88 CA TYR A 50 15.169 73.841 23.947 1.00 38.08 A C ATOM 89 CB TYR A 50 15.264 73.229 25.333 1.00 35.23 A C ATOM 90 CG TYR A 50 16.589 73.472 26.000 1.00 38.28 A C ATOM 91 CD1 TYR A 50 16.881 74.704 26.559 1.00 44.29 A C ATOM 92 CE1 TYR A 50 18.086 74.937 27.171 1.00 45.25 A C ATOM 93 CD2 TYR A 50 17.552 72.470 26.072 1.00 42.25 A C ATOM 94 CE2 TYR A 50 18.758 72.694 26.692 1.00 41.67 A C ATOM 95 CZ TYR A 50 19.015 73.931 27.243 1.00 43.07 A C ATOM 96 OH TYR A 50 20.219 74.182 27.860 1.00 59.73 A O ATOM 97 C TYR A 50 16.397 73.460 23.148 1.00 34.82 A C ATOM 98 O TYR A 50 17.266 74.285 22.910 1.00 34.44 A O ATOM 99 N ARG A 51 16.432 72.195 22.754 1.00 29.73 A N ATOM 100 CA ARG A 51 17.560 71.607 22.057 1.00 37.49 A C ATOM 101 CB ARG A 51 17.249 70.186 21.592 1.00 36.38 A C ATOM 102 CG ARG A 51 18.359 69.583 20.711 1.00 41.48 A C ATOM 103 CD ARG A 51 18.125 68.119 20.377 1.00 39.28 A C ATOM 104 NE ARG A 51 18.422 67.246 21.507 1.00 47.26 A N ATOM 105 CZ ARG A 51 19.632 66.774 21.808 1.00 51.36 A C ATOM 106 NH1 ARG A 51 20.688 67.094 21.059 1.00 47.31 A N ATOM 107 NH2 ARG A 51 19.784 65.983 22.867 1.00 41.13 A N ATOM 108 C ARG A 51 17.934 72.463 20.870 1.00 35.85 A C ATOM 109 O ARG A 51 19.080 72.873 20.721 1.00 35.82 A O ATOM 110 N TYR A 52 16.952 72.756 20.043 1.00 28.40 A N ATOM 111 CA TYR A 52 17.229 73.400 18.775 1.00 30.35 A C ATOM 112 CB TYR A 52 16.339 72.803 17.704 1.00 29.77 A C ATOM 113 CG TYR A 52 16.639 71.337 17.517 1.00 30.95 A C ATOM 114 CD1 TYR A 52 15.635 70.383 17.542 1.00 33.45 A C ATOM 115 CE1 TYR A 52 15.928 69.021 17.383 1.00 34.37 A C ATOM 116 CD2 TYR A 52 17.946 70.899 17.336 1.00 32.23 A C ATOM 117 CE2 TYR A 52 18.246 69.559 17.167 1.00 30.37 A C ATOM 118 CZ TYR A 52 17.239 68.625 17.194 1.00 33.71 A C ATOM 119 OH TYR A 52 17.538 67.296 17.029 1.00 31.94 A O ATOM 120 C TYR A 52 17.246 74.929 18.775 1.00 28.47 A C ATOM 121 O TYR A 52 17.289 75.563 17.712 1.00 28.92 A O ATOM 122 N GLY A 53 17.239 75.515 19.973 1.00 29.71 A N ATOM 123 CA GLY A 53 17.525 76.935 20.140 1.00 34.14 A C ATOM 124 C GLY A 53 16.334 77.846 20.366 1.00 35.57 A C ATOM 125 O GLY A 53 16.475 79.013 20.717 1.00 34.35 A O ATOM 126 N TYR A 54 15.148 77.289 20.189 1.00 34.64 A N ATOM 127 CA TYR A 54 13.912 78.057 20.159 1.00 34.62 A C ATOM 128 CB TYR A 54 12.811 77.139 19.681 1.00 32.63 A C ATOM 129 CG TYR A 54 13.009 76.715 18.256 1.00 27.29 A C ATOM 130 CD1 TYR A 54 13.411 75.425 17.930 1.00 31.05 A C ATOM 131 CE1 TYR A 54 13.596 75.039 16.592 1.00 25.11 A C ATOM 132 CD2 TYR A 54 12.813 77.612 17.226 1.00 28.46 A C ATOM 133 CE2 TYR A 54 12.981 77.233 15.903 1.00 26.56 A C ATOM 134 CZ TYR A 54 13.381 75.952 15.599 1.00 26.82 A C ATOM 135 OH TYR A 54 13.536 75.602 14.273 1.00 27.68 A O ATOM 136 C TYR A 54 13.508 78.745 21.469 1.00 34.35 A C ATOM 137 O TYR A 54 13.030 79.871 21.447 1.00 31.36 A O ATOM 138 N THR A 55 13.731 78.092 22.597 1.00 29.37 A N ATOM 139 CA THR A 55 13.290 78.634 23.869 1.00 33.75 A C ATOM 140 CB THR A 55 13.266 77.561 24.968 1.00 34.33 A C ATOM 141 OG1 THR A 55 14.591 77.335 25.462 1.00 40.91 A O ATOM 142 CG2 THR A 55 12.705 76.268 24.433 1.00 34.63 A C ATOM 143 C THR A 55 14.167 79.809 24.302 1.00 44.98 A C ATOM 144 O THR A 55 13.651 80.823 24.789 1.00 43.86 A O ATOM 145 N ARG A 56 15.482 79.669 24.107 1.00 41.30 A N ATOM 146 CA ARG A 56 16.434 80.747 24.376 1.00 40.16 A C ATOM 147 CB ARG A 56 17.855 80.361 23.923 1.00 45.94 A C ATOM 148 CG ARG A 56 18.395 79.035 24.475 1.00 55.67 A C ATOM 149 CD ARG A 56 19.480 78.405 23.552 1.00 54.23 A C ATOM 150 NE ARG A 56 19.968 77.121 24.068 1.00 50.34 A N ATOM 151 CZ ARG A 56 20.234 76.049 23.317 1.00 51.47 A C ATOM 152 NH1 ARG A 56 20.078 76.091 21.997 1.00 53.10 A N ATOM 153 NH2 ARG A 56 20.656 74.927 23.888 1.00 46.27 A N ATOM 154 C ARG A 56 16.005 82.025 23.654 1.00 38.72 A C ATOM 155 O ARG A 56 16.059 83.109 24.213 1.00 41.62 A O ATOM 156 N VAL A 57 15.590 81.893 22.402 1.00 36.68 A N ATOM 157 CA VAL A 57 15.154 83.039 21.633 1.00 39.39 A C ATOM 158 CB VAL A 57 15.055 82.739 20.127 1.00 34.24 A C ATOM 159 CG1 VAL A 57 14.592 83.985 19.382 1.00 35.58 A C ATOM 160 CG2 VAL A 57 16.415 82.278 19.578 1.00 39.71 A C ATOM 161 C VAL A 57 13.820 83.571 22.145 1.00 39.11 A C ATOM 162 O VAL A 57 13.612 84.779 22.167 1.00 42.74 A O ATOM 163 N GLY A 58 12.916 82.678 22.542 1.00 42.48 A N ATOM 164 CA GLY A 58 11.665 83.094 23.168 1.00 39.23 A C ATOM 165 C GLY A 58 11.963 83.963 24.384 1.00 42.20 A C ATOM 166 O GLY A 58 11.480 85.094 24.501 1.00 44.29 A O ATOM 167 N GLU A 59 12.779 83.440 25.290 1.00 40.15 A N ATOM 168 CA GLU A 59 13.121 84.162 26.505 1.00 40.23 A C ATOM 169 C GLU A 59 13.691 85.519 26.178 1.00 47.82 A C ATOM 170 CB GLU A 59 14.157 83.394 27.313 1.00 43.11 A C ATOM 171 CG GLU A 59 13.833 81.938 27.537 1.00 46.17 A C ATOM 172 CD GLU A 59 14.966 81.224 28.237 1.00 56.40 A C ATOM 173 OE1 GLU A 59 16.028 81.864 28.417 1.00 51.84 A O ATOM 174 OE2 GLU A 59 14.804 80.035 28.609 1.00 59.67 A O ATOM 175 O GLU A 59 13.441 86.493 26.884 1.00 48.47 A O ATOM 176 N MET A 60 14.487 85.560 25.110 1.00 49.65 A N ATOM 177 CA MET A 60 15.200 86.754 24.664 1.00 46.88 A C ATOM 178 C MET A 60 14.199 87.846 24.270 1.00 45.94 A C ATOM 179 CB MET A 60 16.104 86.374 23.473 1.00 50.94 A C ATOM 180 CG MET A 60 17.506 87.008 23.419 1.00 50.81 A C ATOM 181 SD MET A 60 18.720 86.018 22.491 1.00 49.76 A S ATOM 182 CE MET A 60 19.269 84.911 23.778 1.00 46.34 A C ATOM 183 O MET A 60 14.477 89.031 24.400 1.00 44.71 A O ATOM 184 N ARG A 61 13.026 87.432 23.795 1.00 45.78 A N ATOM 185 CA ARG A 61 11.966 88.365 23.408 1.00 47.11 A C ATOM 186 C ARG A 61 10.923 88.517 24.523 1.00 47.89 A C ATOM 187 CB ARG A 61 11.291 87.912 22.105 1.00 44.19 A C ATOM 188 CG ARG A 61 12.268 87.579 20.955 1.00 52.98 A C ATOM 189 CD ARG A 61 11.536 87.268 19.642 1.00 53.56 A C ATOM 190 NE ARG A 61 12.448 86.894 18.555 1.00 56.33 A N ATOM 191 CZ ARG A 61 12.078 86.718 17.285 1.00 56.90 A C ATOM 192 NH1 ARG A 61 12.981 86.383 16.365 1.00 51.19 A N ATOM 193 NH2 ARG A 61 10.808 86.886 16.928 1.00 54.30 A N ATOM 194 O ARG A 61 9.883 89.132 24.317 1.00 48.92 A O ATOM 195 N GLY A 62 11.220 87.942 25.688 1.00 45.01 A N ATOM 196 CA GLY A 62 10.363 88.009 26.862 1.00 52.53 A C ATOM 197 C GLY A 62 9.103 87.153 26.787 1.00 57.24 A C ATOM 198 O GLY A 62 8.040 87.553 27.289 1.00 55.72 A O ATOM 199 N GLU A 63 9.224 85.976 26.177 1.00 48.75 A N ATOM 200 CA GLU A 63 8.068 85.141 25.874 1.00 48.59 A C ATOM 201 C GLU A 63 8.205 83.688 26.343 1.00 51.94 A C ATOM 202 CB GLU A 63 7.753 85.191 24.381 1.00 46.88 A C ATOM 203 CG GLU A 63 7.240 86.537 23.890 1.00 55.37 A C ATOM 204 CD GLU A 63 7.489 86.752 22.400 1.00 56.55 A C ATOM 205 OE1 GLU A 63 8.256 85.961 21.814 1.00 60.14 A O ATOM 206 OE2 GLU A 63 6.936 87.710 21.809 1.00 55.54 A O ATOM 207 O GLU A 63 7.897 82.751 25.600 1.00 49.43 A O ATOM 208 N SER A 64 8.651 83.514 27.586 1.00 54.35 A N ATOM 209 CA SER A 64 8.585 82.226 28.271 1.00 55.77 A C ATOM 210 C SER A 64 7.170 82.051 28.845 1.00 59.60 A C ATOM 211 CB SER A 64 9.633 82.179 29.376 1.00 61.44 A C ATOM 212 OG SER A 64 9.845 83.474 29.921 1.00 63.00 A O ATOM 213 O SER A 64 6.916 81.233 29.735 1.00 55.39 A O ATOM 214 N LYS A 65 6.262 82.860 28.312 1.00 58.51 A N ATOM 215 CA LYS A 65 4.843 82.801 28.615 1.00 60.27 A C ATOM 216 C LYS A 65 4.209 81.577 27.974 1.00 59.18 A C ATOM 217 CB LYS A 65 4.170 84.054 28.049 1.00 59.42 A C ATOM 218 CG LYS A 65 4.702 84.468 26.673 1.00 55.96 A C ATOM 219 CD LYS A 65 4.424 85.936 26.365 1.00 57.92 A C ATOM 220 CE LYS A 65 3.085 86.124 25.664 1.00 66.70 A C ATOM 221 NZ LYS A 65 2.640 87.553 25.620 1.00 68.66 A N ATOM 222 O LYS A 65 3.433 81.710 27.020 1.00 58.45 A O ATOM 223 N SER A 66 4.535 80.394 28.486 1.00 55.49 A N ATOM 224 CA SER A 66 4.076 79.151 27.863 1.00 56.36 A C ATOM 225 C SER A 66 4.816 78.852 26.554 1.00 51.99 A C ATOM 226 CB SER A 66 2.571 79.204 27.589 1.00 50.96 A C ATOM 227 OG SER A 66 2.306 79.735 26.300 1.00 48.57 A O ATOM 228 O SER A 66 5.694 79.610 26.129 1.00 49.63 A O ATOM 229 N LEU A 67 4.428 77.756 25.907 1.00 50.77 A N ATOM 230 CA LEU A 67 5.094 77.286 24.696 1.00 47.17 A C ATOM 231 C LEU A 67 4.764 78.116 23.456 1.00 46.77 A C ATOM 232 CB LEU A 67 4.754 75.809 24.451 1.00 40.25 A C ATOM 233 CG LEU A 67 5.725 74.825 25.090 1.00 40.79 A C ATOM 234 CD1 LEU A 67 5.944 75.156 26.552 1.00 51.23 A C ATOM 235 CD2 LEU A 67 5.226 73.407 24.934 1.00 47.13 A C ATOM 236 O LEU A 67 5.507 78.117 22.459 1.00 38.25 A O ATOM 237 N GLY A 68 3.649 78.826 23.524 1.00 42.27 A N ATOM 238 CA GLY A 68 3.117 79.496 22.359 1.00 38.62 A C ATOM 239 C GLY A 68 4.145 80.148 21.448 1.00 40.35 A C ATOM 240 O GLY A 68 4.326 79.740 20.313 1.00 39.02 A O ATOM 241 N PRO A 69 4.815 81.189 21.936 1.00 38.18 A N ATOM 242 CD PRO A 69 4.841 81.740 23.296 1.00 45.19 A C ATOM 243 CA PRO A 69 5.683 81.928 21.029 1.00 42.35 A C ATOM 244 CB PRO A 69 6.177 83.092 21.896 1.00 46.27 A C ATOM 245 CG PRO A 69 5.198 83.165 23.038 1.00 46.52 A C ATOM 246 C PRO A 69 6.838 81.057 20.482 1.00 37.74 A C ATOM 247 O PRO A 69 7.115 81.154 19.301 1.00 36.74 A O ATOM 248 N ALA A 70 7.456 80.208 21.303 1.00 39.94 A N ATOM 249 CA ALA A 70 8.501 79.288 20.826 1.00 32.70 A C ATOM 250 CB ALA A 70 9.008 78.430 21.967 1.00 34.38 A C ATOM 251 C ALA A 70 8.015 78.405 19.691 1.00 38.37 A C ATOM 252 O ALA A 70 8.718 78.218 18.692 1.00 33.60 A O ATOM 253 N LEU A 71 6.810 77.858 19.828 1.00 31.85 A N ATOM 254 CA LEU A 71 6.265 77.010 18.777 1.00 29.15 A C ATOM 255 CB LEU A 71 4.876 76.523 19.148 1.00 31.24 A C ATOM 256 CG LEU A 71 4.912 75.458 20.219 1.00 30.49 A C ATOM 257 CD1 LEU A 71 3.508 75.225 20.719 1.00 36.69 A C ATOM 258 CD2 LEU A 71 5.482 74.192 19.627 1.00 32.56 A C ATOM 259 C LEU A 71 6.150 77.788 17.496 1.00 32.11 A C ATOM 260 O LEU A 71 6.304 77.243 16.400 1.00 32.86 A O ATOM 261 N LEU A 72 5.827 79.063 17.632 1.00 29.99 A N ATOM 262 CA LEU A 72 5.664 79.892 16.463 1.00 35.28 A C ATOM 263 CB LEU A 72 5.068 81.245 16.839 1.00 35.51 A C ATOM 264 CG LEU A 72 4.357 82.045 15.745 1.00 43.34 A C ATOM 265 CD1 LEU A 72 3.229 81.267 15.088 1.00 42.23 A C ATOM 266 CD2 LEU A 72 3.828 83.344 16.345 1.00 51.30 A C ATOM 267 C LEU A 72 7.028 80.064 15.783 1.00 36.06 A C ATOM 268 O LEU A 72 7.140 79.885 14.584 1.00 35.34 A O ATOM 269 N LEU A 73 8.052 80.400 16.559 1.00 35.18 A N ATOM 270 CA LEU A 73 9.409 80.499 16.017 1.00 37.32 A C ATOM 271 CB LEU A 73 10.419 80.721 17.138 1.00 31.15 A C ATOM 272 CG LEU A 73 10.364 82.098 17.785 1.00 34.21 A C ATOM 273 CD1 LEU A 73 11.406 82.230 18.862 1.00 35.85 A C ATOM 274 CD2 LEU A 73 10.515 83.184 16.741 1.00 43.68 A C ATOM 275 C LEU A 73 9.723 79.218 15.259 1.00 36.24 A C ATOM 276 O LEU A 73 10.181 79.242 14.109 1.00 35.35 A O ATOM 277 N LEU A 74 9.439 78.091 15.893 1.00 32.26 A N ATOM 278 CA LEU A 74 9.656 76.821 15.238 1.00 32.19 A C ATOM 279 CB LEU A 74 9.246 75.669 16.133 1.00 26.76 A C ATOM 280 CG LEU A 74 9.508 74.255 15.620 1.00 25.39 A C ATOM 281 CD1 LEU A 74 9.922 73.403 16.785 1.00 30.67 A C ATOM 282 CD2 LEU A 74 8.270 73.658 14.932 1.00 31.59 A C ATOM 283 C LEU A 74 8.922 76.735 13.928 1.00 35.77 A C ATOM 284 O LEU A 74 9.516 76.429 12.899 1.00 36.31 A O ATOM 285 N GLN A 75 7.621 76.983 13.954 1.00 36.03 A N ATOM 286 CA GLN A 75 6.818 76.769 12.770 1.00 28.91 A C ATOM 287 CB GLN A 75 5.341 77.064 13.048 1.00 33.42 A C ATOM 288 CG GLN A 75 4.611 75.895 13.710 1.00 31.58 A C ATOM 289 CD GLN A 75 3.609 76.340 14.788 1.00 37.14 A C ATOM 290 OE1 GLN A 75 3.265 77.527 14.907 1.00 31.64 A O ATOM 291 NE2 GLN A 75 3.144 75.377 15.575 1.00 34.69 A N ATOM 292 C GLN A 75 7.303 77.573 11.579 1.00 33.24 A C ATOM 293 O GLN A 75 7.252 77.086 10.439 1.00 27.33 A O ATOM 294 N LYS A 76 7.740 78.805 11.813 1.00 31.80 A N ATOM 295 CA LYS A 76 8.254 79.556 10.675 1.00 38.51 A C ATOM 296 CB LYS A 76 8.200 81.066 10.877 1.00 40.13 A C ATOM 297 CG LYS A 76 9.046 81.606 11.980 1.00 43.14 A C ATOM 298 CD LYS A 76 8.398 82.892 12.502 1.00 51.70 A C ATOM 299 CE LYS A 76 6.910 82.654 12.788 1.00 45.31 A C ATOM 300 NZ LYS A 76 6.120 83.912 12.868 1.00 46.65 A N ATOM 301 C LYS A 76 9.647 79.085 10.260 1.00 32.73 A C ATOM 302 O LYS A 76 9.921 78.976 9.085 1.00 33.93 A O ATOM 303 N GLN A 77 10.504 78.768 11.220 1.00 30.80 A N ATOM 304 CA GLN A 77 11.797 78.172 10.882 1.00 38.13 A C ATOM 305 CB GLN A 77 12.618 77.864 12.138 1.00 39.49 A C ATOM 306 CG GLN A 77 14.021 77.262 11.884 1.00 43.07 A C ATOM 307 CD GLN A 77 14.958 78.148 11.033 1.00 41.29 A C ATOM 308 OE1 GLN A 77 15.037 79.379 11.203 1.00 30.40 A O ATOM 309 NE2 GLN A 77 15.685 77.501 10.118 1.00 38.97 A N ATOM 310 C GLN A 77 11.654 76.926 10.005 1.00 35.84 A C ATOM 311 O GLN A 77 12.464 76.710 9.113 1.00 33.90 A O ATOM 312 N LEU A 78 10.606 76.130 10.219 1.00 33.26 A N ATOM 313 CA LEU A 78 10.437 74.902 9.439 1.00 29.13 A C ATOM 314 CB LEU A 78 10.186 73.702 10.338 1.00 27.61 A C ATOM 315 CG LEU A 78 11.234 73.267 11.358 1.00 37.20 A C ATOM 316 CD1 LEU A 78 10.579 72.313 12.364 1.00 36.87 A C ATOM 317 CD2 LEU A 78 12.429 72.594 10.688 1.00 34.07 A C ATOM 318 C LEU A 78 9.355 74.994 8.385 1.00 26.51 A C ATOM 319 O LEU A 78 9.030 74.010 7.708 1.00 30.88 A O ATOM 320 N SER A 79 8.802 76.179 8.203 1.00 26.34 A N ATOM 321 CA SER A 79 7.788 76.347 7.165 1.00 31.27 A C ATOM 322 CB SER A 79 8.385 76.070 5.782 1.00 28.87 A C ATOM 323 OG SER A 79 9.324 77.099 5.458 1.00 36.29 A O ATOM 324 C SER A 79 6.557 75.469 7.438 1.00 29.75 A C ATOM 325 O SER A 79 5.976 74.858 6.539 1.00 26.96 A O ATOM 326 N LEU A 80 6.178 75.427 8.710 1.00 35.15 A N ATOM 327 CA LEU A 80 4.909 74.844 9.131 1.00 29.28 A C ATOM 328 CB LEU A 80 5.106 74.174 10.468 1.00 29.78 A C ATOM 329 CG LEU A 80 6.110 73.031 10.395 1.00 30.57 A C ATOM 330 CD1 LEU A 80 6.277 72.392 11.747 1.00 35.30 A C ATOM 331 CD2 LEU A 80 5.640 72.032 9.377 1.00 33.55 A C ATOM 332 C LEU A 80 3.905 75.971 9.285 1.00 31.11 A C ATOM 333 O LEU A 80 4.282 77.107 9.595 1.00 30.26 A O ATOM 334 N PRO A 81 2.611 75.671 9.099 1.00 36.05 A N ATOM 335 CD PRO A 81 1.965 74.419 8.674 1.00 27.86 A C ATOM 336 CA PRO A 81 1.633 76.744 9.326 1.00 30.12 A C ATOM 337 CB PRO A 81 0.295 76.027 9.150 1.00 33.98 A C ATOM 338 CG PRO A 81 0.639 74.905 8.172 1.00 35.05 A C ATOM 339 C PRO A 81 1.813 77.340 10.722 1.00 27.32 A C ATOM 340 O PRO A 81 2.050 76.621 11.689 1.00 29.98 A O ATOM 341 N GLU A 82 1.775 78.664 10.800 1.00 27.37 A N ATOM 342 CA GLU A 82 2.169 79.364 12.016 1.00 37.44 A C ATOM 343 CB GLU A 82 2.873 80.672 11.638 1.00 37.65 A C ATOM 344 CG GLU A 82 4.101 80.415 10.769 1.00 39.21 A C ATOM 345 CD GLU A 82 4.512 81.591 9.886 1.00 47.26 A C ATOM 346 OE1 GLU A 82 4.234 82.763 10.235 1.00 49.48 A O ATOM 347 OE2 GLU A 82 5.132 81.327 8.833 1.00 47.13 A O ATOM 348 C GLU A 82 0.965 79.586 12.961 1.00 39.29 A C ATOM 349 O GLU A 82 0.231 80.563 12.844 1.00 36.47 A O ATOM 350 N THR A 83 0.771 78.654 13.886 1.00 37.39 A N ATOM 351 CA THR A 83 −0.478 78.586 14.628 1.00 39.83 A C ATOM 352 CB THR A 83 −1.158 77.229 14.436 1.00 35.31 A C ATOM 353 OG1 THR A 83 −0.383 76.213 15.081 1.00 37.39 A O ATOM 354 CG2 THR A 83 −1.250 76.904 12.973 1.00 38.35 A C ATOM 355 C THR A 83 −0.201 78.767 16.090 1.00 41.33 A C ATOM 356 O THR A 83 −1.125 78.912 16.888 1.00 43.93 A O ATOM 357 N GLY A 84 1.079 78.755 16.444 1.00 35.51 A N ATOM 358 CA GLY A 84 1.465 78.949 17.822 1.00 32.99 A C ATOM 359 C GLY A 84 0.877 77.876 18.721 1.00 30.57 A C ATOM 360 O GLY A 84 0.932 77.969 19.943 1.00 36.11 A O ATOM 361 N GLU A 85 0.362 76.830 18.101 1.00 32.47 A N ATOM 362 CA GLU A 85 −0.228 75.714 18.825 1.00 34.29 A C ATOM 363 CB GLU A 85 −1.642 75.444 18.295 1.00 30.31 A C ATOM 364 CG GLU A 85 −2.617 76.580 18.477 1.00 36.66 A C ATOM 365 CD GLU A 85 −3.097 76.731 19.913 1.00 38.33 A C ATOM 366 OE1 GLU A 85 −2.746 75.890 20.773 1.00 35.76 A O ATOM 367 OE2 GLU A 85 −3.823 77.709 20.180 1.00 37.24 A O ATOM 368 C GLU A 85 0.589 74.445 18.643 1.00 33.96 A C ATOM 369 O GLU A 85 1.074 74.168 17.532 1.00 35.36 A O ATOM 370 N LEU A 86 0.723 73.673 19.721 1.00 31.08 A N ATOM 371 CA LEU A 86 1.267 72.329 19.637 1.00 26.04 A C ATOM 372 CB LEU A 86 1.671 71.779 20.998 1.00 31.02 A C ATOM 373 CG LEU A 86 2.158 70.326 20.902 1.00 31.71 A C ATOM 374 CD1 LEU A 86 3.230 70.199 19.829 1.00 39.17 A C ATOM 375 CD2 LEU A 86 2.661 69.809 22.210 1.00 25.92 A C ATOM 376 C LEU A 86 0.264 71.432 18.961 1.00 30.65 A C ATOM 377 O LEU A 86 −0.381 70.596 19.603 1.00 37.54 A O ATOM 378 N ASP A 87 0.131 71.636 17.651 1.00 28.93 A N ATOM 379 CA ASP A 87 −0.803 70.907 16.814 1.00 28.52 A C ATOM 380 CB ASP A 87 −1.338 71.834 15.739 1.00 32.22 A C ATOM 381 CG ASP A 87 −0.244 72.433 14.901 1.00 37.45 A C ATOM 382 OD1 ASP A 87 0.840 71.794 14.831 1.00 32.18 A O ATOM 383 OD2 ASP A 87 −0.483 73.524 14.311 1.00 32.30 A O ATOM 384 C ASP A 87 −0.254 69.641 16.155 1.00 34.31 A C ATOM 385 O ASP A 87 0.844 69.177 16.470 1.00 35.17 A O ATOM 386 N SER A 88 −1.034 69.093 15.233 1.00 28.79 A N ATOM 387 CA SER A 88 −0.706 67.809 14.631 1.00 34.28 A C ATOM 388 CB SER A 88 −1.924 67.249 13.879 1.00 38.31 A C ATOM 389 OG SER A 88 −2.763 66.483 14.729 1.00 36.85 A O ATOM 390 C SER A 88 0.522 67.883 13.690 1.00 36.36 A C ATOM 391 O SER A 88 1.326 66.953 13.630 1.00 30.33 A O ATOM 392 N ALA A 89 0.653 68.985 12.959 1.00 30.55 A N ATOM 393 CA ALA A 89 1.768 69.147 12.029 1.00 33.00 A C ATOM 394 CB ALA A 89 1.526 70.337 11.113 1.00 27.69 A C ATOM 395 C ALA A 89 3.061 69.327 12.817 1.00 32.76 A C ATOM 396 O ALA A 89 4.093 68.740 12.498 1.00 39.05 A O ATOM 397 N THR A 90 2.966 70.114 13.879 1.00 27.95 A N ATOM 398 CA THR A 90 4.087 70.496 14.690 1.00 27.41 A C ATOM 399 CB THR A 90 3.735 71.689 15.559 1.00 27.62 A C ATOM 400 OG1 THR A 90 3.352 72.785 14.706 1.00 24.43 A O ATOM 401 CG2 THR A 90 4.913 72.093 16.404 1.00 26.71 A C ATOM 402 C THR A 90 4.650 69.344 15.501 1.00 34.37 A C ATOM 403 O THR A 90 5.861 69.266 15.724 1.00 29.75 A O ATOM 404 N LEU A 91 3.785 68.422 15.903 1.00 30.38 A N ATOM 405 CA LEU A 91 4.225 67.262 16.654 1.00 28.89 A C ATOM 406 CB LEU A 91 3.063 66.656 17.436 1.00 31.43 A C ATOM 407 CG LEU A 91 3.490 65.460 18.269 1.00 29.96 A C ATOM 408 CD1 LEU A 91 4.115 65.939 19.567 1.00 30.78 A C ATOM 409 CD2 LEU A 91 2.283 64.562 18.567 1.00 43.98 A C ATOM 410 C LEU A 91 4.775 66.206 15.713 1.00 27.77 A C ATOM 411 O LEU A 91 5.695 65.468 16.056 1.00 30.67 A O ATOM 412 N LYS A 92 4.178 66.105 14.537 1.00 25.94 A N ATOM 413 CA LYS A 92 4.706 65.195 13.540 1.00 34.75 A C ATOM 414 CB LYS A 92 3.892 65.329 12.270 1.00 32.15 A C ATOM 415 CG LYS A 92 4.251 64.383 11.159 1.00 40.74 A C ATOM 416 CD LYS A 92 3.801 64.951 9.812 1.00 46.82 A C ATOM 417 CE LYS A 92 3.619 63.853 8.773 1.00 56.66 A C ATOM 418 NZ LYS A 92 3.028 64.390 7.511 1.00 64.71 A N ATOM 419 C LYS A 92 6.192 65.599 13.337 1.00 34.15 A C ATOM 420 O LYS A 92 7.104 64.823 13.636 1.00 36.31 A O ATOM 421 N ALA A 93 6.404 66.835 12.895 1.00 29.82 A N ATOM 422 CA ALA A 93 7.727 67.442 12.787 1.00 30.52 A C ATOM 423 CB ALA A 93 7.620 68.956 12.723 1.00 32.37 A C ATOM 424 C ALA A 93 8.664 67.049 13.908 1.00 31.47 A C ATOM 425 O ALA A 93 9.730 66.535 13.652 1.00 34.91 A O ATOM 426 N MET A 94 8.260 67.278 15.152 1.00 32.27 A N ATOM 427 CA MET A 94 9.137 67.070 16.291 1.00 28.69 A C ATOM 428 CB MET A 94 8.491 67.585 17.574 1.00 31.80 A C ATOM 429 CG MET A 94 8.318 69.096 17.627 1.00 34.44 A C ATOM 430 SD MET A 94 7.363 69.556 19.088 1.00 33.84 A S ATOM 431 CE MET A 94 7.826 71.262 19.413 1.00 27.02 A C ATOM 432 C MET A 94 9.538 65.619 16.470 1.00 31.18 A C ATOM 433 O MET A 94 10.525 65.321 17.141 1.00 34.01 A O ATOM 434 N ARG A 95 8.761 64.721 15.885 1.00 27.55 A N ATOM 435 CA ARG A 95 9.067 63.298 15.969 1.00 32.87 A C ATOM 436 CB ARG A 95 7.776 62.465 15.900 1.00 40.23 A C ATOM 437 CG ARG A 95 6.920 62.333 17.183 1.00 47.14 A C ATOM 438 CD ARG A 95 5.945 61.138 17.041 1.00 43.71 A C ATOM 439 NE ARG A 95 4.902 61.101 18.066 1.00 60.66 A N ATOM 440 CZ ARG A 95 3.604 61.308 17.833 1.00 53.96 A C ATOM 441 NH1 ARG A 95 3.172 61.566 16.599 1.00 48.81 A N ATOM 442 NH2 ARG A 95 2.736 61.252 18.838 1.00 51.57 A N ATOM 443 C ARG A 95 9.944 62.851 14.796 1.00 30.91 A C ATOM 444 O ARG A 95 10.353 61.700 14.735 1.00 31.59 A O ATOM 445 N THR A 96 10.162 63.733 13.825 1.00 35.13 A N ATOM 446 CA THR A 96 10.887 63.341 12.615 1.00 35.74 A C ATOM 447 CB THR A 96 10.611 64.291 11.465 1.00 36.83 A C ATOM 448 OG1 THR A 96 9.212 64.264 11.161 1.00 36.09 A O ATOM 449 CG2 THR A 96 11.381 63.850 10.218 1.00 36.82 A C ATOM 450 C THR A 96 12.396 63.258 12.880 1.00 26.10 A C ATOM 451 O THR A 96 12.962 64.113 13.559 1.00 28.48 A O ATOM 452 N PRO A 97 13.038 62.186 12.396 1.00 32.24 A N ATOM 453 CD PRO A 97 12.419 60.981 11.820 1.00 33.02 A C ATOM 454 CA PRO A 97 14.507 62.066 12.470 1.00 26.77 A C ATOM 455 CB PRO A 97 14.786 60.824 11.636 1.00 29.53 A C ATOM 456 CG PRO A 97 13.564 59.989 11.828 1.00 35.14 A C ATOM 457 C PRO A 97 15.186 63.293 11.854 1.00 24.73 A C ATOM 458 O PRO A 97 14.630 63.871 10.927 1.00 27.34 A O ATOM 459 N ARG A 98 16.347 63.701 12.365 1.00 30.20 A N ATOM 460 CA ARG A 98 16.959 64.928 11.865 1.00 25.00 A C ATOM 461 CB ARG A 98 16.109 66.137 12.252 1.00 27.45 A C ATOM 462 CG ARG A 98 16.117 66.422 13.778 1.00 25.11 A C ATOM 463 CD ARG A 98 15.671 67.865 14.047 1.00 32.74 A C ATOM 464 NE ARG A 98 16.776 68.825 14.005 1.00 26.80 A N ATOM 465 CZ ARG A 98 16.637 70.144 13.849 1.00 28.52 A C ATOM 466 NH1 ARG A 98 15.446 70.689 13.695 1.00 21.59 A N ATOM 467 NH2 ARG A 98 17.706 70.928 13.831 1.00 31.24 A N ATOM 468 C ARG A 98 18.371 65.175 12.359 1.00 25.55 A C ATOM 469 O ARG A 98 18.914 64.438 13.175 1.00 26.91 A O ATOM 470 N CYS A 99 18.934 66.268 11.864 1.00 27.95 A N ATOM 471 CA CYS A 99 20.286 66.678 12.162 1.00 23.49 A C ATOM 472 CB CYS A 99 20.730 67.683 11.094 1.00 28.07 A C ATOM 473 SG CYS A 99 22.327 68.447 11.402 1.00 25.26 A S ATOM 474 C CYS A 99 20.401 67.317 13.530 1.00 28.48 A C ATOM 475 O CYS A 99 19.598 68.169 13.879 1.00 26.25 A O ATOM 476 N GLY A 100 21.448 66.958 14.270 1.00 20.70 A N ATOM 477 CA GLY A 100 21.630 67.456 15.618 1.00 25.18 A C ATOM 478 C GLY A 100 22.034 68.905 15.760 1.00 25.21 A C ATOM 479 O GLY A 100 22.166 69.427 16.887 1.00 21.18 A O ATOM 480 N VAL A 101 22.271 69.573 14.637 1.00 25.63 A N ATOM 481 CA VAL A 101 22.720 70.960 14.739 1.00 29.99 A C ATOM 482 CB VAL A 101 23.422 71.468 13.442 1.00 27.85 A C ATOM 483 CG1 VAL A 101 23.647 73.004 13.520 1.00 29.85 A C ATOM 484 CG2 VAL A 101 24.747 70.744 13.213 1.00 21.36 A C ATOM 485 C VAL A 101 21.521 71.856 15.026 1.00 27.56 A C ATOM 486 O VAL A 101 20.471 71.664 14.441 1.00 27.84 A O ATOM 487 N PRO A 102 21.702 72.869 15.891 1.00 27.71 A N ATOM 488 CD PRO A 102 22.795 72.845 16.868 1.00 28.78 A C ATOM 489 CA PRO A 102 20.726 73.910 16.220 1.00 26.25 A C ATOM 490 CB PRO A 102 21.476 74.774 17.226 1.00 31.38 A C ATOM 491 CG PRO A 102 22.335 73.819 17.919 1.00 34.27 A C ATOM 492 C PRO A 102 20.221 74.764 15.075 1.00 35.16 A C ATOM 493 O PRO A 102 21.011 75.264 14.280 1.00 35.13 A O ATOM 494 N ASP A 103 18.897 74.947 15.025 1.00 31.26 A N ATOM 495 CA ASP A 103 18.251 75.791 14.036 1.00 31.08 A C ATOM 496 CB ASP A 103 16.752 75.465 13.951 1.00 26.77 A C ATOM 497 CG ASP A 103 16.517 74.046 13.650 1.00 31.77 A C ATOM 498 OD1 ASP A 103 17.475 73.380 13.186 1.00 30.48 A O ATOM 499 OD2 ASP A 103 15.385 73.583 13.857 1.00 29.34 A O ATOM 500 C ASP A 103 18.424 77.279 14.324 1.00 28.28 A C ATOM 501 O ASP A 103 18.409 78.076 13.400 1.00 29.08 A O ATOM 502 N LEU A 104 18.545 77.643 15.601 1.00 32.53 A N ATOM 503 CA LEU A 104 18.744 79.036 15.994 1.00 35.19 A C ATOM 504 CB LEU A 104 17.458 79.671 16.550 1.00 34.65 A C ATOM 505 CG LEU A 104 16.154 79.698 15.737 1.00 37.22 A C ATOM 506 CD1 LEU A 104 15.107 80.581 16.451 1.00 33.05 A C ATOM 507 CD2 LEU A 104 16.323 80.179 14.304 1.00 33.29 A C ATOM 508 C LEU A 104 19.859 79.141 17.022 1.00 33.55 A C ATOM 509 O LEU A 104 19.935 78.347 17.955 1.00 37.79 A O ATOM 510 N GLY A 105 20.741 80.118 16.847 1.00 35.96 A N ATOM 511 CA GLY A 105 21.908 80.191 17.701 1.00 43.35 A C ATOM 512 C GLY A 105 22.852 79.052 17.357 1.00 40.89 A C ATOM 513 O GLY A 105 22.741 78.436 16.288 1.00 37.69 A O ATOM 514 N ARG A 106 23.749 78.732 18.279 1.00 44.31 A N ATOM 515 CA ARG A 106 24.917 77.939 17.937 1.00 46.80 A C ATOM 516 CB ARG A 106 26.125 78.876 17.927 1.00 52.01 A C ATOM 517 CG ARG A 106 27.269 78.438 17.054 1.00 51.48 A C ATOM 518 CD ARG A 106 27.087 78.888 15.605 1.00 55.60 A C ATOM 519 NE ARG A 106 27.004 80.340 15.470 1.00 49.14 A N ATOM 520 CZ ARG A 106 26.764 80.958 14.320 1.00 55.22 A C ATOM 521 NH1 ARG A 106 26.599 80.243 13.209 1.00 48.94 A N ATOM 522 NH2 ARG A 106 26.691 82.287 14.280 1.00 55.01 A N ATOM 523 C ARG A 106 25.170 76.824 18.941 1.00 46.89 A C ATOM 524 O ARG A 106 24.764 76.930 20.095 1.00 46.93 A O ATOM 525 N PHE A 107 25.836 75.754 18.509 1.00 38.00 A N ATOM 526 CA PHE A 107 26.393 74.794 19.463 1.00 42.73 A C ATOM 527 CB PHE A 107 27.459 73.924 18.796 1.00 42.91 A C ATOM 528 CG PHE A 107 26.929 72.691 18.118 1.00 41.68 A C ATOM 529 CD1 PHE A 107 26.050 71.838 18.767 1.00 48.54 A C ATOM 530 CD2 PHE A 107 27.362 72.352 16.852 1.00 36.91 A C ATOM 531 CE1 PHE A 107 25.584 70.671 18.136 1.00 43.24 A C ATOM 532 CE2 PHE A 107 26.917 71.207 16.222 1.00 35.72 A C ATOM 533 CZ PHE A 107 26.023 70.360 16.866 1.00 41.92 A C ATOM 534 C PHE A 107 27.059 75.526 20.635 1.00 43.91 A C ATOM 535 O PHE A 107 26.775 75.261 21.809 1.00 44.08 A O ATOM 536 N GLN A 108 27.960 76.446 20.307 1.00 44.68 A N ATOM 537 CA GLN A 108 28.763 77.137 21.316 1.00 43.81 A C ATOM 538 CB GLN A 108 29.946 76.266 21.704 1.00 41.88 A C ATOM 539 CG GLN A 108 30.818 75.953 20.521 1.00 41.69 A C ATOM 540 CD GLN A 108 31.846 74.903 20.825 1.00 46.11 A C ATOM 541 OE1 GLN A 108 31.511 73.769 21.175 1.00 49.23 A O ATOM 542 NE2 GLN A 108 33.114 75.268 20.693 1.00 44.02 A N ATOM 543 C GLN A 108 29.310 78.419 20.737 1.00 42.16 A C ATOM 544 O GLN A 108 28.969 78.792 19.610 1.00 42.43 A O ATOM 545 N THR A 109 30.162 79.097 21.503 1.00 40.78 A N ATOM 546 CA THR A 109 30.969 80.154 20.920 1.00 39.66 A C ATOM 547 CB THR A 109 31.512 81.125 21.963 1.00 43.06 A C ATOM 548 OG1 THR A 109 30.578 82.202 22.134 1.00 37.58 A O ATOM 549 CG2 THR A 109 32.843 81.699 21.483 1.00 44.17 A C ATOM 550 C THR A 109 32.116 79.521 20.132 1.00 42.69 A C ATOM 551 O THR A 109 32.802 78.624 20.630 1.00 37.60 A O ATOM 552 N PHE A 110 32.295 79.977 18.895 1.00 43.05 A N ATOM 553 CA PHE A 110 33.260 79.384 17.974 1.00 34.07 A C ATOM 554 CB PHE A 110 32.572 78.902 16.706 1.00 29.70 A C ATOM 555 CG PHE A 110 31.830 77.613 16.875 1.00 41.66 A C ATOM 556 CD1 PHE A 110 30.448 77.572 16.785 1.00 36.10 A C ATOM 557 CD2 PHE A 110 32.515 76.441 17.134 1.00 36.95 A C ATOM 558 CE1 PHE A 110 29.780 76.391 16.927 1.00 36.92 A C ATOM 559 CE2 PHE A 110 31.839 75.245 17.278 1.00 38.60 A C ATOM 560 CZ PHE A 110 30.474 75.226 17.179 1.00 38.96 A C ATOM 561 C PHE A 110 34.337 80.380 17.589 1.00 43.28 A C ATOM 562 O PHE A 110 34.148 81.594 17.698 1.00 42.92 A O ATOM 563 N GLU A 111 35.469 79.855 17.130 1.00 43.23 A N ATOM 564 CA GLU A 111 36.589 80.697 16.754 1.00 43.68 A C ATOM 565 CB GLU A 111 37.898 79.980 17.025 1.00 44.45 A C ATOM 566 CG GLU A 111 38.465 80.266 18.382 1.00 54.53 A C ATOM 567 CD GLU A 111 39.950 79.991 18.435 1.00 63.27 A C ATOM 568 OE1 GLU A 111 40.531 79.614 17.384 1.00 57.56 A O ATOM 569 OE2 GLU A 111 40.536 80.159 19.526 1.00 70.29 A O ATOM 570 C GLU A 111 36.540 81.137 15.302 1.00 40.37 A C ATOM 571 O GLU A 111 36.296 80.331 14.392 1.00 38.14 A O ATOM 572 N GLY A 112 36.774 82.427 15.091 1.00 39.63 A N ATOM 573 CA GLY A 112 36.947 82.950 13.752 1.00 39.53 A C ATOM 574 C GLY A 112 35.713 83.285 12.945 1.00 41.53 A C ATOM 575 O GLY A 112 34.663 83.644 13.472 1.00 46.71 A O ATOM 576 N ASP A 113 35.878 83.127 11.638 1.00 40.89 A N ATOM 577 CA ASP A 113 34.987 83.594 10.592 1.00 45.20 A C ATOM 578 CB ASP A 113 35.818 83.731 9.313 1.00 44.17 A C ATOM 579 CG ASP A 113 35.491 84.961 8.551 1.00 51.40 A C ATOM 580 OD1 ASP A 113 35.099 85.950 9.202 1.00 57.77 A O ATOM 581 OD2 ASP A 113 35.629 84.946 7.313 1.00 49.39 A O ATOM 582 C ASP A 113 33.836 82.627 10.279 1.00 43.98 A C ATOM 583 O ASP A 113 32.791 83.045 9.786 1.00 39.87 A O ATOM 584 N LEU A 114 34.070 81.338 10.516 1.00 38.94 A N ATOM 585 CA LEU A 114 33.129 80.280 10.151 1.00 39.63 A C ATOM 586 CB LEU A 114 31.706 80.585 10.611 1.00 36.54 A C ATOM 587 CG LEU A 114 31.557 80.974 12.077 1.00 35.18 A C ATOM 588 CD1 LEU A 114 30.085 80.957 12.402 1.00 44.40 A C ATOM 589 CD2 LEU A 114 32.330 80.038 13.005 1.00 37.15 A C ATOM 590 C LEU A 114 33.155 80.071 8.663 1.00 38.62 A C ATOM 591 O LEU A 114 32.226 79.510 8.084 1.00 35.10 A O ATOM 592 N LYS A 115 34.255 80.518 8.061 1.00 40.38 A N ATOM 593 CA LYS A 115 34.535 80.374 6.634 1.00 41.06 A C ATOM 594 CB LYS A 115 34.592 81.773 6.019 1.00 43.32 A C ATOM 595 CG LYS A 115 34.270 81.858 4.557 1.00 42.22 A C ATOM 596 CD LYS A 115 34.565 83.250 4.022 1.00 46.15 A C ATOM 597 CE LYS A 115 33.946 84.322 4.910 1.00 50.64 A C ATOM 598 NZ LYS A 115 34.188 85.701 4.389 1.00 57.92 A N ATOM 599 C LYS A 115 35.920 79.717 6.513 1.00 36.01 A C ATOM 600 O LYS A 115 36.787 79.986 7.335 1.00 34.55 A O ATOM 601 N TRP A 116 36.134 78.842 5.534 1.00 32.72 A N ATOM 602 CA TRP A 116 37.505 78.376 5.307 1.00 39.30 A C ATOM 603 CB TRP A 116 37.586 77.105 4.468 1.00 35.24 A C ATOM 604 CG TRP A 116 37.099 75.883 5.157 1.00 34.99 A C ATOM 605 CD2 TRP A 116 37.642 75.271 6.330 1.00 31.07 A C ATOM 606 CE2 TRP A 116 36.859 74.139 6.604 1.00 27.78 A C ATOM 607 CE3 TRP A 116 38.700 75.572 7.174 1.00 33.71 A C ATOM 608 CD1 TRP A 116 36.058 75.113 4.776 1.00 29.26 A C ATOM 609 NE1 TRP A 116 35.915 74.057 5.628 1.00 27.19 A N ATOM 610 CZ2 TRP A 116 37.101 73.303 7.675 1.00 29.81 A C ATOM 611 CZ3 TRP A 116 38.939 74.744 8.254 1.00 38.41 A C ATOM 612 CH2 TRP A 116 38.137 73.628 8.501 1.00 36.13 A C ATOM 613 C TRP A 116 38.279 79.480 4.620 1.00 39.17 A C ATOM 614 O TRP A 116 37.698 80.306 3.915 1.00 44.17 A O ATOM 615 N HIS A 117 39.591 79.503 4.823 1.00 42.50 A N ATOM 616 CA HIS A 117 40.399 80.531 4.192 1.00 40.42 A C ATOM 617 CB HIS A 117 40.818 81.586 5.211 1.00 42.18 A C ATOM 618 CG HIS A 117 39.740 82.573 5.523 1.00 45.02 A C ATOM 619 CD2 HIS A 117 39.153 83.522 4.755 1.00 47.90 A C ATOM 620 ND1 HIS A 117 39.113 82.631 6.751 1.00 51.58 A N ATOM 621 CE1 HIS A 117 38.205 83.590 6.735 1.00 48.59 A C ATOM 622 NE2 HIS A 117 38.206 84.144 5.534 1.00 53.43 A N ATOM 623 C HIS A 117 41.579 79.933 3.448 1.00 40.46 A C ATOM 624 O HIS A 117 42.644 80.535 3.351 1.00 35.38 A O ATOM 625 N HIS A 118 41.362 78.724 2.945 1.00 38.35 A N ATOM 626 CA HIS A 118 42.234 78.102 1.964 1.00 38.52 A C ATOM 627 CB HIS A 118 43.338 77.262 2.615 1.00 36.85 A C ATOM 628 CG HIS A 118 42.843 76.138 3.478 1.00 38.63 A C ATOM 629 CD2 HIS A 118 42.636 74.828 3.199 1.00 36.76 A C ATOM 630 ND1 HIS A 118 42.556 76.297 4.819 1.00 35.53 A N ATOM 631 CE1 HIS A 118 42.185 75.131 5.327 1.00 36.89 A C ATOM 632 NE2 HIS A 118 42.223 74.225 4.365 1.00 32.95 A N ATOM 633 C HIS A 118 41.375 77.263 1.055 1.00 41.51 A C ATOM 634 O HIS A 118 40.261 76.870 1.420 1.00 38.65 A O ATOM 635 N HIS A 119 41.890 76.995 −0.129 1.00 32.72 A N ATOM 636 CA HIS A 119 41.090 76.430 −1.178 1.00 37.57 A C ATOM 637 CB HIS A 119 41.643 76.877 −2.531 1.00 44.33 A C ATOM 638 CG HIS A 119 41.185 76.034 −3.677 1.00 47.43 A C ATOM 639 CD2 HIS A 119 41.548 74.789 −4.070 1.00 49.60 A C ATOM 640 ND1 HIS A 119 40.209 76.446 −4.560 1.00 48.63 A N ATOM 641 CE1 HIS A 119 39.997 75.496 −5.454 1.00 42.14 A C ATOM 642 NE2 HIS A 119 40.791 74.477 −5.176 1.00 49.26 A N ATOM 643 C HIS A 119 41.046 74.913 −1.096 1.00 36.29 A C ATOM 644 O HIS A 119 40.122 74.289 −1.603 1.00 41.61 A O ATOM 645 N ASN A 120 42.043 74.293 −0.486 1.00 37.40 A N ATOM 646 CA ASN A 120 42.062 72.838 −0.543 1.00 36.57 A C ATOM 647 CB ASN A 120 43.369 72.284 −1.098 1.00 36.51 A C ATOM 648 CG ASN A 120 43.344 70.779 −1.185 1.00 42.43 A C ATOM 649 OD1 ASN A 120 42.299 70.160 −0.954 1.00 38.80 A O ATOM 650 ND2 ASN A 120 44.488 70.171 −1.500 1.00 40.90 A N ATOM 651 C ASN A 120 41.761 72.217 0.791 1.00 33.50 A C ATOM 652 O ASN A 120 42.576 72.251 1.712 1.00 34.03 A O ATOM 653 N ILE A 121 40.568 71.642 0.895 1.00 35.59 A N ATOM 654 CA ILE A 121 40.101 71.162 2.184 1.00 32.53 A C ATOM 655 CB ILE A 121 38.567 71.419 2.371 1.00 29.15 A C ATOM 656 CG2 ILE A 121 38.169 71.248 3.824 1.00 29.28 A C ATOM 657 CG1 ILE A 121 38.209 72.832 1.898 1.00 26.11 A C ATOM 658 CD1 ILE A 121 38.869 73.938 2.685 1.00 30.14 A C ATOM 659 C ILE A 121 40.478 69.701 2.305 1.00 24.26 A C ATOM 660 O ILE A 121 40.269 68.910 1.393 1.00 33.22 A O ATOM 661 N THR A 122 41.063 69.335 3.421 1.00 26.54 A N ATOM 662 CA THR A 122 41.529 67.971 3.555 1.00 30.49 A C ATOM 663 CB THR A 122 42.938 67.947 4.120 1.00 28.73 A C ATOM 664 OG1 THR A 122 42.957 68.701 5.334 1.00 28.29 A O ATOM 665 CG2 THR A 122 43.925 68.591 3.115 1.00 27.70 A C ATOM 666 C THR A 122 40.619 67.286 4.549 1.00 30.80 A C ATOM 667 O THR A 122 40.196 67.906 5.516 1.00 31.77 A O ATOM 668 N TYR A 123 40.350 66.010 4.332 1.00 27.41 A N ATOM 669 CA TYR A 123 39.517 65.289 5.270 1.00 35.48 A C ATOM 670 CB TYR A 123 38.094 65.147 4.718 1.00 22.88 A C ATOM 671 CG TYR A 123 37.921 64.201 3.548 1.00 26.64 A C ATOM 672 CD1 TYR A 123 38.073 64.648 2.251 1.00 24.67 A C ATOM 673 CE1 TYR A 123 37.886 63.797 1.180 1.00 28.01 A C ATOM 674 CD2 TYR A 123 37.576 62.865 3.747 1.00 25.90 A C ATOM 675 CE2 TYR A 123 37.372 62.012 2.690 1.00 24.39 A C ATOM 676 CZ TYR A 123 37.531 62.483 1.404 1.00 26.57 A C ATOM 677 OH TYR A 123 37.339 61.643 0.335 1.00 31.98 A O ATOM 678 C TYR A 123 40.076 63.932 5.641 1.00 33.76 A C ATOM 679 O TYR A 123 40.627 63.224 4.792 1.00 30.17 A O ATOM 680 N TRP A 124 39.913 63.582 6.917 1.00 29.77 A N ATOM 681 CA TRP A 124 40.322 62.287 7.420 1.00 30.90 A C ATOM 682 CB TRP A 124 41.338 62.484 8.536 1.00 33.31 A C ATOM 683 CG TRP A 124 41.802 61.213 9.098 1.00 32.64 A C ATOM 684 CD2 TRP A 124 42.165 60.971 10.452 1.00 33.00 A C ATOM 685 CE2 TRP A 124 42.546 59.630 10.548 1.00 30.03 A C ATOM 686 CE3 TRP A 124 42.196 61.767 11.604 1.00 38.82 A C ATOM 687 CD1 TRP A 124 41.982 60.046 8.433 1.00 35.71 A C ATOM 688 NE1 TRP A 124 42.431 59.079 9.300 1.00 35.41 A N ATOM 689 CZ2 TRP A 124 42.955 59.060 11.740 1.00 37.70 A C ATOM 690 CZ3 TRP A 124 42.601 61.207 12.786 1.00 41.30 A C ATOM 691 CH2 TRP A 124 42.983 59.866 12.849 1.00 36.32 A C ATOM 692 C TRP A 124 39.161 61.423 7.939 1.00 34.90 A C ATOM 693 O TRP A 124 38.497 61.785 8.909 1.00 34.00 A O ATOM 694 N ILE A 125 38.942 60.280 7.291 1.00 37.00 A N ATOM 695 CA ILE A 125 37.977 59.291 7.741 1.00 31.41 A C ATOM 696 CB ILE A 125 37.657 58.299 6.646 1.00 34.68 A C ATOM 697 CG2 ILE A 125 36.643 57.275 7.138 1.00 36.59 A C ATOM 698 CG1 ILE A 125 37.145 59.020 5.401 1.00 29.29 A C ATOM 699 CD1 ILE A 125 36.882 58.081 4.247 1.00 34.65 A C ATOM 700 C ILE A 125 38.572 58.504 8.887 1.00 36.09 A C ATOM 701 O ILE A 125 39.229 57.476 8.672 1.00 34.90 A O ATOM 702 N GLN A 126 38.301 58.977 10.100 1.00 34.47 A N ATOM 703 CA GLN A 126 38.937 58.502 11.322 1.00 32.52 A C ATOM 704 CB GLN A 126 38.693 59.505 12.442 1.00 29.79 A C ATOM 705 CG GLN A 126 39.092 58.998 13.797 1.00 36.48 A C ATOM 706 CD GLN A 126 39.092 60.098 14.840 1.00 46.68 A C ATOM 707 OE1 GLN A 126 38.041 60.625 15.202 1.00 47.95 A O ATOM 708 NE2 GLN A 126 40.278 60.450 15.335 1.00 46.62 A N ATOM 709 C GLN A 126 38.527 57.088 11.767 1.00 38.02 A C ATOM 710 O GLN A 126 39.320 56.374 12.384 1.00 38.26 A O ATOM 711 N ASN A 127 37.304 56.671 11.452 1.00 31.21 A N ATOM 712 CA ASN A 127 36.851 55.338 11.823 1.00 33.38 A C ATOM 713 CB ASN A 127 36.541 55.265 13.322 1.00 36.21 A C ATOM 714 CG ASN A 127 35.288 56.048 13.704 1.00 35.75 A C ATOM 715 OD1 ASN A 127 34.454 56.351 12.860 1.00 35.10 A O ATOM 716 ND2 ASN A 127 35.164 56.374 14.973 1.00 36.01 A N ATOM 717 C ASN A 127 35.646 54.924 10.991 1.00 36.66 A C ATOM 718 O ASN A 127 35.153 55.706 10.183 1.00 38.05 A O ATOM 719 N TYR A 128 35.170 53.702 11.178 1.00 33.81 A N ATOM 720 CA TYR A 128 34.075 53.213 10.354 1.00 35.75 A C ATOM 721 CB TYR A 128 34.596 52.173 9.376 1.00 34.70 A C ATOM 722 CG TYR A 128 35.500 52.750 8.309 1.00 40.93 A C ATOM 723 CD1 TYR A 128 35.035 52.930 7.012 1.00 41.68 A C ATOM 724 CE1 TYR A 128 35.848 53.449 6.016 1.00 42.35 A C ATOM 725 CD2 TYR A 128 36.821 53.109 8.590 1.00 41.17 A C ATOM 726 CE2 TYR A 128 37.646 53.637 7.594 1.00 38.98 A C ATOM 727 CZ TYR A 128 37.146 53.800 6.308 1.00 40.91 A C ATOM 728 OH TYR A 128 37.913 54.320 5.296 1.00 36.87 A O ATOM 729 C TYR A 128 32.935 52.614 11.184 1.00 39.01 A C ATOM 730 O TYR A 128 33.136 52.232 12.334 1.00 40.17 A O ATOM 731 N SER A 129 31.747 52.522 10.593 1.00 32.23 A N ATOM 732 CA SER A 129 30.713 51.687 11.177 1.00 37.41 A C ATOM 733 CB SER A 129 29.349 52.359 11.119 1.00 30.18 A C ATOM 734 OG SER A 129 28.587 51.810 10.065 1.00 31.57 A O ATOM 735 C SER A 129 30.687 50.416 10.365 1.00 37.57 A C ATOM 736 O SER A 129 30.980 50.431 9.162 1.00 37.79 A O ATOM 737 N GLU A 130 30.341 49.322 11.029 1.00 34.53 A N ATOM 738 CA GLU A 130 30.345 48.001 10.421 1.00 37.20 A C ATOM 739 CB GLU A 130 30.510 46.941 11.513 1.00 37.94 A C ATOM 740 CG GLU A 130 31.854 46.998 12.217 1.00 41.66 A C ATOM 741 CD GLU A 130 33.025 46.755 11.252 1.00 48.61 A C ATOM 742 OE1 GLU A 130 32.871 45.961 10.298 1.00 43.12 A O ATOM 743 OE2 GLU A 130 34.098 47.363 11.449 1.00 53.13 A O ATOM 744 C GLU A 130 29.084 47.715 9.624 1.00 37.89 A C ATOM 745 O GLU A 130 28.899 46.589 9.146 1.00 37.01 A O ATOM 746 N ASP A 131 28.215 48.720 9.488 1.00 33.20 A N ATOM 747 CA ASP A 131 26.983 48.561 8.707 1.00 30.26 A C ATOM 748 CB ASP A 131 26.019 49.735 8.965 1.00 34.52 A C ATOM 749 CG ASP A 131 25.491 49.763 10.399 1.00 34.43 A C ATOM 750 OD1 ASP A 131 25.435 48.691 11.038 1.00 32.61 A O ATOM 751 OD2 ASP A 131 25.149 50.859 10.891 1.00 36.69 A O ATOM 752 C ASP A 131 27.211 48.398 7.195 1.00 33.84 A C ATOM 753 O ASP A 131 26.350 47.867 6.490 1.00 27.26 A O ATOM 754 N LEU A 132 28.360 48.865 6.694 1.00 33.49 A N ATOM 755 CA LEU A 132 28.676 48.815 5.256 1.00 28.02 A C ATOM 756 CB LEU A 132 28.387 50.178 4.610 1.00 32.60 A C ATOM 757 CG LEU A 132 26.962 50.728 4.447 1.00 33.16 A C ATOM 758 CD1 LEU A 132 26.938 52.272 4.335 1.00 27.49 A C ATOM 759 CD2 LEU A 132 26.255 50.068 3.243 1.00 30.78 A C ATOM 760 C LEU A 132 30.176 48.483 5.066 1.00 31.60 A C ATOM 761 O LEU A 132 30.979 48.683 5.984 1.00 30.76 A O ATOM 762 N PRO A 133 30.558 47.985 3.872 1.00 26.11 A N ATOM 763 CD PRO A 133 29.715 47.660 2.716 1.00 27.42 A C ATOM 764 CA PRO A 133 31.987 47.811 3.575 1.00 32.72 A C ATOM 765 CB PRO A 133 31.984 47.291 2.131 1.00 33.38 A C ATOM 766 CG PRO A 133 30.578 46.730 1.920 1.00 31.29 A C ATOM 767 C PRO A 133 32.678 49.166 3.613 1.00 31.48 A C ATOM 768 O PRO A 133 32.057 50.157 3.249 1.00 32.54 A O ATOM 769 N ARG A 134 33.935 49.218 4.029 1.00 36.40 A N ATOM 770 CA ARG A 134 34.631 50.498 4.091 1.00 33.95 A C ATOM 771 CB ARG A 134 35.998 50.330 4.735 1.00 39.76 A C ATOM 772 CG ARG A 134 35.931 49.574 6.035 1.00 40.80 A C ATOM 773 CD ARG A 134 37.091 49.941 6.934 1.00 43.02 A C ATOM 774 NE ARG A 134 37.139 49.059 8.092 1.00 47.95 A N ATOM 775 CZ ARG A 134 38.118 49.065 8.989 1.00 56.39 A C ATOM 776 NH1 ARG A 134 39.133 49.911 8.852 1.00 53.66 A N ATOM 777 NH2 ARG A 134 38.082 48.226 10.021 1.00 63.92 A N ATOM 778 C ARG A 134 34.747 51.143 2.713 1.00 33.12 A C ATOM 779 O ARG A 134 34.786 52.367 2.582 1.00 35.74 A O ATOM 780 N ALA A 135 34.769 50.331 1.675 1.00 29.57 A N ATOM 781 CA ALA A 135 34.844 50.918 0.351 1.00 34.30 A C ATOM 782 CB ALA A 135 35.038 49.858 −0.681 1.00 31.50 A C ATOM 783 C ALA A 135 33.564 51.717 0.076 1.00 38.91 A C ATOM 784 O ALA A 135 33.612 52.883 −0.328 1.00 37.81 A O ATOM 785 N VAL A 136 32.414 51.088 0.302 1.00 36.67 A N ATOM 786 CA VAL A 136 31.135 51.769 0.096 1.00 34.10 A C ATOM 787 CB VAL A 136 29.937 50.808 0.327 1.00 38.81 A C ATOM 788 CG1 VAL A 136 28.624 51.582 0.514 1.00 33.80 A C ATOM 789 CG2 VAL A 136 29.826 49.833 −0.833 1.00 36.47 A C ATOM 790 C VAL A 136 31.025 53.043 0.953 1.00 27.14 A C ATOM 791 O VAL A 136 30.426 54.016 0.546 1.00 32.83 A O ATOM 792 N ILE A 137 31.630 53.035 2.123 1.00 28.43 A N ATOM 793 CA ILE A 137 31.632 54.209 2.979 1.00 27.95 A C ATOM 794 CB ILE A 137 32.041 53.814 4.410 1.00 29.11 A C ATOM 795 CG2 ILE A 137 32.410 55.027 5.248 1.00 26.72 A C ATOM 796 CG1 ILE A 137 30.928 52.989 5.079 1.00 33.40 A C ATOM 797 CD1 ILE A 137 31.136 52.731 6.570 1.00 31.36 A C ATOM 798 C ILE A 137 32.591 55.278 2.437 1.00 36.02 A C ATOM 799 O ILE A 137 32.291 56.481 2.430 1.00 27.71 A O ATOM 800 N ASP A 138 33.759 54.848 1.974 1.00 33.80 A N ATOM 801 CA ASP A 138 34.672 55.804 1.371 1.00 32.70 A C ATOM 802 CB ASP A 138 35.932 55.102 0.865 1.00 33.99 A C ATOM 803 CG ASP A 138 36.727 54.481 1.966 1.00 33.09 A C ATOM 804 OD1 ASP A 138 36.580 54.906 3.127 1.00 40.74 A O ATOM 805 OD2 ASP A 138 37.523 53.564 1.667 1.00 41.65 A O ATOM 806 C ASP A 138 34.004 56.519 0.207 1.00 24.67 A C ATOM 807 O ASP A 138 34.052 57.726 0.110 1.00 30.11 A O ATOM 808 N ASP A 139 33.399 55.765 −0.697 1.00 28.10 A N ATOM 809 CA ASP A 139 32.860 56.354 −1.918 1.00 25.82 A C ATOM 810 CB ASP A 139 32.415 55.245 −2.845 1.00 32.24 A C ATOM 811 CG ASP A 139 31.411 55.705 −3.866 1.00 37.67 A C ATOM 812 OD1 ASP A 139 31.813 56.333 −4.864 1.00 44.46 A O ATOM 813 OD2 ASP A 139 30.210 55.403 −3.698 1.00 42.63 A O ATOM 814 C ASP A 139 31.672 57.246 −1.599 1.00 35.16 A C ATOM 815 O ASP A 139 31.431 58.275 −2.254 1.00 31.91 A O ATOM 816 N ALA A 140 30.916 56.828 −0.588 1.00 32.89 A N ATOM 817 CA ALA A 140 29.780 57.607 −0.115 1.00 33.14 A C ATOM 818 CB ALA A 140 29.081 56.881 1.045 1.00 28.65 A C ATOM 819 C ALA A 140 30.254 58.988 0.306 1.00 27.26 A C ATOM 820 O ALA A 140 29.680 59.993 −0.096 1.00 31.78 A O ATOM 821 N PHE A 141 31.318 59.060 1.091 1.00 30.08 A N ATOM 822 CA PHE A 141 31.840 60.379 1.468 1.00 29.18 A C ATOM 823 CB PHE A 141 32.908 60.271 2.555 1.00 34.53 A C ATOM 824 CG PHE A 141 32.394 59.794 3.885 1.00 30.07 A C ATOM 825 CD1 PHE A 141 31.193 60.271 4.402 1.00 32.94 A C ATOM 826 CD2 PHE A 141 33.123 58.886 4.636 1.00 27.72 A C ATOM 827 CE1 PHE A 141 30.725 59.839 5.647 1.00 29.84 A C ATOM 828 CE2 PHE A 141 32.663 58.450 5.879 1.00 36.22 A C ATOM 829 CZ PHE A 141 31.456 58.930 6.381 1.00 30.44 A C ATOM 830 C PHE A 141 32.375 61.180 0.261 1.00 30.34 A C ATOM 831 O PHE A 141 32.163 62.393 0.162 1.00 28.80 A O ATOM 832 N ALA A 142 33.053 60.506 −0.666 1.00 33.51 A N ATOM 833 CA ALA A 142 33.626 61.209 −1.818 1.00 34.14 A C ATOM 834 CB ALA A 142 34.462 60.244 −2.669 1.00 35.98 A C ATOM 835 C ALA A 142 32.533 61.837 −2.664 1.00 31.34 A C ATOM 836 O ALA A 142 32.592 63.018 −3.023 1.00 29.07 A O ATOM 837 N ARG A 143 31.526 61.024 −2.978 1.00 30.48 A N ATOM 838 CA ARG A 143 30.402 61.466 −3.786 1.00 24.34 A C ATOM 839 CB ARG A 143 29.385 60.351 −3.933 1.00 25.55 A C ATOM 840 CG ARG A 143 29.802 59.309 −4.940 1.00 31.09 A C ATOM 841 CD ARG A 143 29.180 57.984 −4.657 1.00 32.69 A C ATOM 842 NE ARG A 143 27.737 58.094 −4.638 1.00 40.43 A N ATOM 843 CZ ARG A 143 26.930 57.638 −3.678 1.00 39.04 A C ATOM 844 NH1 ARG A 143 27.386 56.971 −2.618 1.00 32.01 A N ATOM 845 NH2 ARG A 143 25.632 57.833 −3.814 1.00 36.43 A N ATOM 846 C ARG A 143 29.766 62.687 −3.164 1.00 23.70 A C ATOM 847 O ARG A 143 29.383 63.611 −3.873 1.00 27.78 A O ATOM 848 N ALA A 144 29.680 62.680 −1.834 1.00 23.70 A N ATOM 849 CA ALA A 144 29.153 63.793 −1.046 1.00 25.97 A C ATOM 850 CB ALA A 144 29.077 63.389 0.446 1.00 27.89 A C ATOM 851 C ALA A 144 29.950 65.092 −1.205 1.00 28.68 A C ATOM 852 O ALA A 144 29.371 66.168 −1.421 1.00 23.37 A O ATOM 853 N PHE A 145 31.276 64.997 −1.080 1.00 31.53 A N ATOM 854 CA PHE A 145 32.163 66.143 −1.372 1.00 24.45 A C ATOM 855 CB PHE A 145 33.610 65.843 −0.986 1.00 24.66 A C ATOM 856 CG PHE A 145 33.861 65.844 0.491 1.00 27.82 A C ATOM 857 CD1 PHE A 145 33.697 67.002 1.233 1.00 25.76 A C ATOM 858 CD2 PHE A 145 34.296 64.692 1.139 1.00 28.43 A C ATOM 859 CE1 PHE A 145 33.945 67.005 2.583 1.00 24.95 A C ATOM 860 CE2 PHE A 145 34.560 64.692 2.484 1.00 26.00 A C ATOM 861 CZ PHE A 145 34.384 65.851 3.214 1.00 28.47 A C ATOM 862 C PHE A 145 32.093 66.539 −2.833 1.00 20.85 A C ATOM 863 O PHE A 145 32.064 67.719 −3.172 1.00 28.89 A O ATOM 864 N ALA A 146 32.008 65.562 −3.715 1.00 21.83 A N ATOM 865 CA ALA A 146 31.899 65.877 −5.125 1.00 20.02 A C ATOM 866 CB ALA A 146 31.807 64.597 −5.918 1.00 23.54 A C ATOM 867 C ALA A 146 30.683 66.787 −5.429 1.00 29.66 A C ATOM 868 O ALA A 146 30.646 67.499 −6.443 1.00 21.03 A O ATOM 869 N LEU A 147 29.676 66.754 −4.559 1.00 24.91 A N ATOM 870 CA LEU A 147 28.467 67.554 −4.783 1.00 26.36 A C ATOM 871 CB LEU A 147 27.367 67.211 −3.751 1.00 19.44 A C ATOM 872 CG LEU A 147 26.396 66.078 −4.041 1.00 26.97 A C ATOM 873 CD1 LEU A 147 25.309 66.087 −2.947 1.00 25.48 A C ATOM 874 CD2 LEU A 147 25.739 66.210 −5.399 1.00 28.06 A C ATOM 875 C LEU A 147 28.813 69.010 −4.621 1.00 18.74 A C ATOM 876 O LEU A 147 28.347 69.866 −5.365 1.00 24.03 A O ATOM 877 N TRP A 148 29.611 69.269 −3.609 1.00 20.20 A N ATOM 878 CA TRP A 148 29.969 70.612 −3.235 1.00 26.06 A C ATOM 879 CB TRP A 148 30.372 70.628 −1.772 1.00 23.77 A C ATOM 880 CG TRP A 148 29.203 70.424 −0.789 1.00 33.02 A C ATOM 881 CD2 TRP A 148 28.042 71.260 −0.646 1.00 31.64 A C ATOM 882 CE2 TRP A 148 27.234 70.693 0.371 1.00 35.58 A C ATOM 883 CE3 TRP A 148 27.605 72.432 −1.279 1.00 30.31 A C ATOM 884 CD1 TRP A 148 29.062 69.415 0.131 1.00 31.57 A C ATOM 885 NE1 TRP A 148 27.882 69.571 0.833 1.00 31.61 A N ATOM 886 CZ2 TRP A 148 26.018 71.270 0.776 1.00 28.98 A C ATOM 887 CZ3 TRP A 148 26.377 73.000 −0.881 1.00 33.29 A C ATOM 888 CH2 TRP A 148 25.614 72.423 0.138 1.00 25.14 A C ATOM 889 C TRP A 148 31.126 71.186 −4.068 1.00 32.74 A C ATOM 890 O TRP A 148 31.112 72.364 −4.421 1.00 32.85 A O ATOM 891 N SER A 149 32.154 70.381 −4.330 1.00 29.94 A N ATOM 892 CA SER A 149 33.290 70.894 −5.098 1.00 31.65 A C ATOM 893 CB SER A 149 34.344 69.814 −5.318 1.00 28.83 A C ATOM 894 OG SER A 149 34.016 69.090 −6.475 1.00 33.07 A O ATOM 895 C SER A 149 32.830 71.484 −6.440 1.00 26.72 A C ATOM 896 O SER A 149 33.318 72.520 −6.855 1.00 30.94 A O ATOM 897 N ALA A 150 31.857 70.864 −7.096 1.00 22.46 A N ATOM 898 CA ALA A 150 31.381 71.397 −8.356 1.00 21.16 A C ATOM 899 CB ALA A 150 30.466 70.430 −9.041 1.00 24.22 A C ATOM 900 C ALA A 150 30.738 72.778 −8.290 1.00 25.46 A C ATOM 901 O ALA A 150 30.531 73.407 −9.321 1.00 28.00 A O ATOM 902 N VAL A 151 30.423 73.270 −7.100 1.00 27.77 A N ATOM 903 CA VAL A 151 29.690 74.536 −7.032 1.00 27.42 A C ATOM 904 CB VAL A 151 28.229 74.326 −6.585 1.00 26.49 A C ATOM 905 CG1 VAL A 151 27.450 73.668 −7.692 1.00 19.47 A C ATOM 906 CG2 VAL A 151 28.169 73.466 −5.314 1.00 26.32 A C ATOM 907 C VAL A 151 30.433 75.499 −6.143 1.00 25.99 A C ATOM 908 O VAL A 151 30.035 76.641 −5.936 1.00 30.72 A O ATOM 909 N THR A 152 31.544 75.014 −5.618 1.00 32.49 A N ATOM 910 CA THR A 152 32.448 75.849 −4.854 1.00 36.18 A C ATOM 911 CB THR A 152 32.697 75.243 −3.491 1.00 36.45 A C ATOM 912 OG1 THR A 152 32.922 73.841 −3.663 1.00 39.67 A O ATOM 913 CG2 THR A 152 31.486 75.457 −2.589 1.00 32.17 A C ATOM 914 C THR A 152 33.803 75.962 −5.546 1.00 37.62 A C ATOM 915 O THR A 152 34.173 75.119 −6.363 1.00 35.91 A O ATOM 916 N PRO A 153 34.542 77.019 −5.215 1.00 34.09 A N ATOM 917 CD PRO A 153 34.098 78.153 −4.393 1.00 43.15 A C ATOM 918 CA PRO A 153 35.939 77.151 −5.603 1.00 41.47 A C ATOM 919 CB PRO A 153 36.218 78.642 −5.403 1.00 45.96 A C ATOM 920 CG PRO A 153 34.903 79.265 −4.940 1.00 46.62 A C ATOM 921 C PRO A 153 36.729 76.395 −4.571 1.00 41.21 A C ATOM 922 O PRO A 153 37.607 76.998 −3.955 1.00 46.60 A O ATOM 923 N LEU A 154 36.400 75.126 −4.346 1.00 36.26 A N ATOM 924 CA LEU A 154 37.089 74.343 −3.324 1.00 35.56 A C ATOM 925 CB LEU A 154 36.243 74.223 −2.044 1.00 35.17 A C ATOM 926 CG LEU A 154 35.900 75.468 −1.205 1.00 35.37 A C ATOM 927 CD1 LEU A 154 35.239 75.063 0.094 1.00 32.76 A C ATOM 928 CD2 LEU A 154 37.114 76.330 −0.887 1.00 37.91 A C ATOM 929 C LEU A 154 37.369 72.960 −3.861 1.00 31.93 A C ATOM 930 O LEU A 154 36.638 72.472 −4.730 1.00 31.78 A O ATOM 931 N THR A 155 38.412 72.323 −3.331 1.00 28.79 A N ATOM 932 CA THR A 155 38.700 70.928 −3.649 1.00 25.34 A C ATOM 933 CB THR A 155 40.087 70.738 −4.318 1.00 29.53 A C ATOM 934 OG1 THR A 155 41.069 71.454 −3.557 1.00 30.87 A O ATOM 935 CG2 THR A 155 40.067 71.228 −5.718 1.00 31.71 A C ATOM 936 C THR A 155 38.796 70.197 −2.345 1.00 24.14 A C ATOM 937 O THR A 155 39.165 70.785 −1.338 1.00 27.05 A O ATOM 938 N PHE A 156 38.515 68.903 −2.367 1.00 27.88 A N ATOM 939 CA PHE A 156 38.548 68.143 −1.132 1.00 32.96 A C ATOM 940 CB PHE A 156 37.129 67.653 −0.747 1.00 27.70 A C ATOM 941 CG PHE A 156 36.109 68.757 −0.727 1.00 24.80 A C ATOM 942 CD1 PHE A 156 35.253 68.939 −1.791 1.00 27.20 A C ATOM 943 CD2 PHE A 156 36.023 69.617 0.359 1.00 25.70 A C ATOM 944 CE1 PHE A 156 34.332 69.979 −1.791 1.00 27.11 A C ATOM 945 CE2 PHE A 156 35.122 70.650 0.367 1.00 24.81 A C ATOM 946 CZ PHE A 156 34.272 70.831 −0.710 1.00 22.28 A C ATOM 947 C PHE A 156 39.520 66.998 −1.285 1.00 24.20 A C ATOM 948 O PHE A 156 39.541 66.341 −2.310 1.00 28.04 A O ATOM 949 N THR A 157 40.271 66.728 −0.232 1.00 25.89 A N ATOM 950 CA THR A 157 41.365 65.788 −0.322 1.00 31.86 A C ATOM 951 CB THR A 157 42.709 66.551 −0.442 1.00 32.50 A C ATOM 952 OG1 THR A 157 42.710 67.316 −1.657 1.00 36.08 A O ATOM 953 CG2 THR A 157 43.863 65.593 −0.452 1.00 33.63 A C ATOM 954 C THR A 157 41.414 64.881 0.886 1.00 27.21 A C ATOM 955 O THR A 157 41.542 65.355 2.009 1.00 30.08 A O ATOM 956 N ARG A 158 41.342 63.572 0.644 1.00 32.23 A N ATOM 957 CA ARG A 158 41.426 62.571 1.718 1.00 32.19 A C ATOM 958 CB ARG A 158 40.914 61.215 1.231 1.00 26.93 A C ATOM 959 CG ARG A 158 41.059 60.120 2.278 1.00 28.30 A C ATOM 960 CD ARG A 158 40.355 58.843 1.864 1.00 28.04 A C ATOM 961 NE ARG A 158 40.433 57.856 2.933 1.00 30.93 A N ATOM 962 CZ ARG A 158 40.130 56.570 2.780 1.00 29.89 A C ATOM 963 NH1 ARG A 158 39.727 56.117 1.605 1.00 28.69 A N ATOM 964 NH2 ARG A 158 40.235 55.739 3.804 1.00 32.90 A N ATOM 965 C ARG A 158 42.849 62.404 2.258 1.00 34.84 A C ATOM 966 O ARG A 158 43.766 62.117 1.491 1.00 38.24 A O ATOM 967 N VAL A 159 43.005 62.584 3.568 1.00 34.25 A N ATOM 968 CA VAL A 159 44.270 62.410 4.278 1.00 37.44 A C ATOM 969 CB VAL A 159 44.711 63.701 4.969 1.00 35.19 A C ATOM 970 CG1 VAL A 159 44.866 64.833 3.956 1.00 35.82 A C ATOM 971 CG2 VAL A 159 43.726 64.076 6.059 1.00 37.83 A C ATOM 972 C VAL A 159 44.160 61.360 5.389 1.00 41.92 A C ATOM 973 O VAL A 159 43.136 60.670 5.517 1.00 35.74 A O ATOM 974 N TYR A 160 45.206 61.270 6.217 1.00 42.62 A N ATOM 975 CA TYR A 160 45.280 60.218 7.221 1.00 37.36 A C ATOM 976 CB TYR A 160 46.061 59.037 6.648 1.00 37.40 A C ATOM 977 CG TYR A 160 45.340 58.392 5.486 1.00 37.03 A C ATOM 978 CD1 TYR A 160 45.572 58.798 4.168 1.00 36.62 A C ATOM 979 CE1 TYR A 160 44.888 58.202 3.099 1.00 30.90 A C ATOM 980 CD2 TYR A 160 44.401 57.389 5.704 1.00 40.75 A C ATOM 981 CE2 TYR A 160 43.721 56.794 4.652 1.00 33.36 A C ATOM 982 CZ TYR A 160 43.967 57.198 3.364 1.00 38.05 A C ATOM 983 OH TYR A 160 43.270 56.587 2.353 1.00 38.34 A O ATOM 984 C TYR A 160 45.829 60.660 8.582 1.00 39.74 A C ATOM 985 O TYR A 160 46.569 59.926 9.235 1.00 45.57 A O ATOM 986 N SER A 161 45.423 61.839 9.037 1.00 39.44 A N ATOM 987 CA SER A 161 45.941 62.383 10.289 1.00 43.72 A C ATOM 988 CB SER A 161 47.311 63.034 10.048 1.00 45.57 A C ATOM 989 OG SER A 161 47.174 64.396 9.643 1.00 42.49 A O ATOM 990 C SER A 161 45.005 63.416 10.951 1.00 44.50 A C ATOM 991 O SER A 161 44.185 64.049 10.297 1.00 39.35 A O ATOM 992 N ARG A 162 45.171 63.604 12.251 1.00 43.86 A N ATOM 993 CA ARG A 162 44.362 64.537 13.013 1.00 49.09 A C ATOM 994 CB ARG A 162 44.869 64.575 14.459 1.00 56.78 A C ATOM 995 CG ARG A 162 44.900 65.960 15.104 1.00 60.00 A C ATOM 226 CD ARG A 162 45.987 66.028 16.185 1.00 65.00 A C ATOM 997 NE ARG A 162 47.209 65.323 15.785 1.00 63.48 A N ATOM 998 CZ ARG A 162 48.211 65.038 16.613 1.00 66.17 A C ATOM 999 NH1 ARG A 162 48.129 65.400 17.889 1.00 66.79 A N ATOM 1000 NH2 ARG A 162 49.290 64.391 16.173 1.00 54.98 A N ATOM 1001 C ARG A 162 44.352 65.944 12.429 1.00 49.92 A C ATOM 1002 O ARG A 162 43.561 66.793 12.844 1.00 52.42 A O ATOM 1003 N ASP A 163 45.229 66.203 11.468 1.00 49.74 A N ATOM 1004 CA ASP A 163 45.400 67.572 11.001 1.00 51.36 A C ATOM 1005 CB ASP A 163 46.876 67.871 10.719 1.00 55.95 A C ATOM 1006 CG ASP A 163 47.579 68.507 11.916 1.00 62.51 A C ATOM 1007 OD1 ASP A 163 47.383 68.025 13.056 1.00 65.84 A O ATOM 1008 OD2 ASP A 163 48.325 69.492 11.716 1.00 61.80 A O ATOM 1009 C ASP A 163 44.528 67.941 9.804 1.00 45.41 A C ATOM 1010 O ASP A 163 44.629 69.045 9.271 1.00 45.19 A O ATOM 1011 N ALA A 164 43.675 67.022 9.379 1.00 41.14 A N ATOM 1012 CA ALA A 164 42.716 67.349 8.341 1.00 30.81 A C ATOM 1013 CB ALA A 164 41.845 66.161 8.065 1.00 31.83 A C ATOM 1014 C ALA A 164 41.879 68.539 8.798 1.00 34.75 A C ATOM 1015 O ALA A 164 41.721 68.780 9.990 1.00 36.03 A O ATOM 1016 N ASP A 165 41.373 69.307 7.847 1.00 35.52 A N ATOM 1017 CA ASP A 165 40.397 70.338 8.158 1.00 31.35 A C ATOM 1018 CB ASP A 165 40.003 71.066 6.885 1.00 31.60 A C ATOM 1019 CG ASP A 165 41.189 71.784 6.230 1.00 31.34 A C ATOM 1020 OD1 ASP A 165 42.002 72.358 6.969 1.00 33.79 A O ATOM 1021 OD2 ASP A 165 41.286 71.784 4.994 1.00 31.29 A O ATOM 1022 C ASP A 165 39.161 69.669 8.747 1.00 34.46 A C ATOM 1023 O ASP A 165 38.687 70.065 9.811 1.00 32.22 A O ATOM 1024 N ILE A 166 38.654 68.655 8.042 1.00 26.44 A N ATOM 1025 CA ILE A 166 37.435 67.963 8.431 1.00 32.49 A C ATOM 1026 CB ILE A 166 36.437 67.909 7.255 1.00 34.03 A C ATOM 1027 CG2 ILE A 166 35.079 67.373 7.715 1.00 34.49 A C ATOM 1028 CG1 ILE A 166 36.287 69.280 6.598 1.00 29.50 A C ATOM 1029 CD1 ILE A 166 35.276 69.300 5.467 1.00 33.82 A C ATOM 1030 C ILE A 166 37.693 66.525 8.896 1.00 30.25 A C ATOM 1031 O ILE A 166 37.920 65.640 8.084 1.00 31.28 A O ATOM 1032 N VAL A 167 37.635 66.294 10.204 1.00 30.76 A N ATOM 1033 CA VAL A 167 37.708 64.931 10.716 1.00 31.12 A C ATOM 1034 CB VAL A 167 38.392 64.874 12.057 1.00 26.77 A C ATOM 1035 CG1 VAL A 167 38.581 63.420 12.459 1.00 29.40 A C ATOM 1036 CG2 VAL A 167 39.732 65.608 12.008 1.00 28.08 A C ATOM 1037 C VAL A 167 36.327 64.257 10.833 1.00 35.95 A C ATOM 1038 O VAL A 167 35.396 64.801 11.428 1.00 33.05 A O ATOM 1039 N ILE A 168 36.225 63.067 10.263 1.00 34.26 A N ATOM 1040 CA ILE A 168 34.972 62.330 10.150 1.00 34.47 A C ATOM 1041 CB ILE A 168 34.782 61.839 8.726 1.00 31.38 A C ATOM 1042 CG2 ILE A 168 33.608 60.887 8.610 1.00 32.51 A C ATOM 1043 CG1 ILE A 168 34.567 63.025 7.802 1.00 29.00 A C ATOM 1044 CD1 ILE A 168 34.199 62.597 6.407 1.00 35.00 A C ATOM 1045 C ILE A 168 34.988 61.130 11.096 1.00 39.82 A C ATOM 1046 O ILE A 168 35.946 60.331 11.119 1.00 31.84 A O ATOM 1047 N GLN A 169 33.916 61.012 11.872 1.00 34.48 A N ATOM 1048 CA GLN A 169 33.849 60.068 12.980 1.00 31.39 A C ATOM 1049 CB GLN A 169 34.186 60.799 14.264 1.00 35.93 A C ATOM 1050 CG GLN A 169 34.348 59.920 15.458 1.00 40.30 A C ATOM 1051 CD GLN A 169 34.957 60.674 16.603 1.00 47.43 A C ATOM 1052 OE1 GLN A 169 35.733 61.609 16.392 1.00 49.96 A O ATOM 1053 NE2 GLN A 169 34.612 60.286 17.828 1.00 50.08 A N ATOM 1054 C GLN A 169 32.461 59.450 13.109 1.00 34.84 A C ATOM 1055 O GLN A 169 31.447 60.141 13.005 1.00 38.71 A O ATOM 1056 N PHE A 170 32.415 58.143 13.310 1.00 30.95 A N ATOM 1057 CA PHE A 170 31.185 57.501 13.725 1.00 37.19 A C ATOM 1058 CB PHE A 170 31.009 56.153 13.062 1.00 31.97 A C ATOM 1059 CG PHE A 170 30.914 56.214 11.568 1.00 35.47 A C ATOM 1060 CD1 PHE A 170 32.041 56.447 10.796 1.00 33.00 A C ATOM 1061 CD2 PHE A 170 29.701 56.014 10.929 1.00 31.61 A C ATOM 1062 CE1 PHE A 170 31.963 56.481 9.416 1.00 32.08 A C ATOM 1063 CE2 PHE A 170 29.615 56.045 9.550 1.00 30.52 A C ATOM 1064 CZ PHE A 170 30.747 56.281 8.789 1.00 31.95 A C ATOM 1065 C PHE A 170 31.289 57.309 15.222 1.00 39.74 A C ATOM 1066 O PHE A 170 32.346 56.925 15.736 1.00 33.16 A O ATOM 1067 N GLY A 171 30.196 57.572 15.922 1.00 31.71 A N ATOM 1068 CA GLY A 171 30.187 57.434 17.372 1.00 36.21 A C ATOM 1069 C GLY A 171 28.816 57.129 17.963 1.00 34.75 A C ATOM 1070 O GLY A 171 27.809 57.086 17.225 1.00 35.88 A O ATOM 1071 N VAL A 172 28.776 56.903 19.283 1.00 38.73 A N ATOM 1072 CA VAL A 172 27.507 56.716 20.003 1.00 36.61 A C ATOM 1073 CB VAL A 172 27.221 55.243 20.367 1.00 35.51 A C ATOM 1074 CG1 VAL A 172 26.864 54.445 19.147 1.00 32.42 A C ATOM 1075 CG2 VAL A 172 28.408 54.650 21.081 1.00 41.39 A C ATOM 1076 C VAL A 172 27.474 57.504 21.294 1.00 39.89 A C ATOM 1077 O VAL A 172 28.504 57.739 21.931 1.00 41.29 A O ATOM 1078 N ALA A 173 26.272 57.919 21.675 1.00 41.08 A N ATOM 1079 CA ALA A 173 26.084 58.517 22.976 1.00 42.22 A C ATOM 1080 CB ALA A 173 26.255 57.473 24.041 1.00 41.24 A C ATOM 1081 C ALA A 173 27.133 59.589 23.127 1.00 39.63 A C ATOM 1082 O ALA A 173 27.348 60.385 22.217 1.00 39.45 A O ATOM 1083 N GLU A 174 27.789 59.616 24.277 1.00 40.86 A N ATOM 1084 CA GLU A 174 28.902 60.535 24.429 1.00 48.13 A C ATOM 1085 CB GLU A 174 29.227 60.821 25.885 1.00 45.08 A C ATOM 1086 CG GLU A 174 30.487 61.666 26.023 1.00 46.91 A C ATOM 1087 CD GLU A 174 30.399 62.983 25.263 1.00 48.50 A C ATOM 1088 OE1 GLU A 174 29.808 63.021 24.153 1.00 51.41 A O ATOM 1089 OE2 GLU A 174 30.936 63.991 25.773 1.00 54.97 A O ATOM 1090 C GLU A 174 30.136 59.990 23.724 1.00 45.16 A C ATOM 1091 O GLU A 174 30.664 58.923 24.079 1.00 39.72 A O ATOM 1092 N HIS A 175 30.604 60.746 22.740 1.00 42.65 A N ATOM 1093 CA HIS A 175 31.686 60.295 21.874 1.00 39.48 A C ATOM 1094 CB HIS A 175 31.128 60.040 20.483 1.00 42.18 A C ATOM 1095 CG HIS A 175 30.431 61.225 19.899 1.00 40.69 A C ATOM 1096 CD2 HIS A 175 30.364 61.679 18.629 1.00 44.05 A C ATOM 1097 ND1 HIS A 175 29.699 62.108 20.661 1.00 44.14 A N ATOM 1098 CE1 HIS A 175 29.213 63.056 19.884 1.00 41.54 A C ATOM 1099 NE2 HIS A 175 29.598 62.816 18.645 1.00 38.50 A N ATOM 1100 C HIS A 175 32.870 61.277 21.827 1.00 44.29 A C ATOM 1101 O HIS A 175 33.678 61.263 20.896 1.00 40.22 A O ATOM 1102 N GLY A 176 32.965 62.136 22.825 1.00 38.00 A N ATOM 1103 CA GLY A 176 34.185 62.884 23.021 1.00 42.71 A C ATOM 1104 C GLY A 176 34.085 64.380 22.859 1.00 45.76 A C ATOM 1105 O GLY A 176 35.089 65.073 23.035 1.00 46.26 A O ATOM 1106 N ASP A 177 32.898 64.890 22.528 1.00 43.51 A N ATOM 1107 CA ASP A 177 32.777 66.331 22.270 1.00 45.89 A C ATOM 1108 CB ASP A 177 32.415 66.625 20.808 1.00 40.81 A C ATOM 1109 CG ASP A 177 31.151 65.920 20.348 1.00 39.85 A C ATOM 1110 OD1 ASP A 177 30.454 65.285 21.172 1.00 40.46 A O ATOM 1111 OD2 ASP A 177 30.865 66.016 19.140 1.00 28.10 A O ATOM 1112 C ASP A 177 31.858 67.127 23.196 1.00 47.53 A C ATOM 1113 O ASP A 177 31.838 68.352 23.111 1.00 44.07 A O ATOM 1114 N GLY A 178 31.113 66.443 24.068 1.00 52.24 A N ATOM 1115 CA GLY A 178 30.147 67.106 24.942 1.00 48.03 A C ATOM 1116 C GLY A 178 28.830 67.454 24.260 1.00 45.80 A C ATOM 1117 O GLY A 178 28.063 68.292 24.740 1.00 50.76 A O ATOM 1118 N TYR A 179 28.592 66.824 23.118 1.00 39.99 A N ATOM 1119 CA TYR A 179 27.320 66.887 22.433 1.00 38.05 A C ATOM 1120 CB TYR A 179 27.426 67.711 21.150 1.00 37.84 A C ATOM 1121 CG TYR A 179 27.826 69.148 21.387 1.00 46.63 A C ATOM 1122 CD1 TYR A 179 29.165 69.498 21.552 1.00 42.26 A C ATOM 1123 CE1 TYR A 179 29.545 70.804 21.774 1.00 45.26 A C ATOM 1124 CD2 TYR A 179 26.874 70.156 21.453 1.00 45.56 A C ATOM 1125 CE2 TYR A 179 27.249 71.477 21.672 1.00 48.97 A C ATOM 1126 CZ TYR A 179 28.587 71.788 21.833 1.00 42.42 A C ATOM 1127 OH TYR A 179 28.968 73.083 22.054 1.00 48.46 A O ATOM 1128 C TYR A 179 26.941 65.444 22.108 1.00 40.86 A C ATOM 1129 O TYR A 179 27.033 65.012 20.963 1.00 43.07 A O ATOM 1130 N PRO A 180 26.512 64.694 23.127 1.00 41.83 A N ATOM 1131 CD PRO A 180 26.199 65.239 24.460 1.00 44.60 A C ATOM 1132 CA PRO A 180 26.247 63.256 23.036 1.00 42.09 A C ATOM 1133 CB PRO A 180 25.755 62.897 24.445 1.00 43.93 A C ATOM 1134 CG PRO A 180 26.215 64.020 25.330 1.00 46.79 A C ATOM 1135 C PRO A 180 25.158 62.931 22.037 1.00 35.93 A C ATOM 1136 O PRO A 180 24.256 63.721 21.827 1.00 33.90 A O ATOM 1137 N PHE A 181 25.257 61.776 21.405 1.00 35.55 A N ATOM 1138 CA PHE A 181 24.176 61.302 20.577 1.00 34.50 A C ATOM 1139 CB PHE A 181 24.688 60.320 19.538 1.00 36.99 A C ATOM 1140 CG PHE A 181 25.388 60.984 18.381 1.00 39.75 A C ATOM 1141 CD1 PHE A 181 24.748 61.969 17.642 1.00 35.92 A C ATOM 1142 CD2 PHE A 181 26.680 60.622 18.027 1.00 41.58 A C ATOM 1143 CE1 PHE A 181 25.382 62.579 16.570 1.00 42.20 A C ATOM 1144 CE2 PHE A 181 27.316 61.234 16.965 1.00 35.23 A C ATOM 1145 CZ PHE A 181 26.669 62.210 16.233 1.00 34.90 A C ATOM 1146 C PHE A 181 23.129 60.664 21.494 1.00 39.63 A C ATOM 1147 O PHE A 181 23.317 60.617 22.713 1.00 36.58 A O ATOM 1148 N ASP A 182 22.048 60.172 20.903 1.00 37.05 A N ATOM 1149 CA ASP A 182 20.852 59.822 21.650 1.00 38.32 A C ATOM 1150 CB ASP A 182 19.803 60.898 21.396 1.00 31.69 A C ATOM 1151 CG ASP A 182 19.381 60.953 19.946 1.00 38.75 A C ATOM 1152 OD1 ASP A 182 19.959 60.207 19.136 1.00 39.74 A O ATOM 1153 OD2 ASP A 182 18.476 61.735 19.596 1.00 41.97 A O ATOM 1154 C ASP A 182 20.276 58.461 21.261 1.00 40.11 A C ATOM 1155 O ASP A 182 19.060 58.275 21.279 1.00 39.50 A O ATOM 1156 N GLY A 183 21.135 57.509 20.905 1.00 36.64 A N ATOM 1157 CA GLY A 183 20.676 56.162 20.592 1.00 29.13 A C ATOM 1158 C GLY A 183 19.854 56.184 19.329 1.00 38.57 A C ATOM 1159 O GLY A 183 19.841 57.200 18.640 1.00 39.70 A O ATOM 1160 N LYS A 184 19.139 55.098 19.035 1.00 35.06 A N ATOM 1161 CA LYS A 184 18.525 54.946 17.717 1.00 33.16 A C ATOM 1162 CB LYS A 184 17.859 53.579 17.561 1.00 36.65 A C ATOM 1163 CG LYS A 184 17.603 53.207 16.111 1.00 38.12 A C ATOM 1164 CD LYS A 184 16.993 51.823 15.961 1.00 37.42 A C ATOM 1165 CE LYS A 184 15.551 51.937 15.526 1.00 41.09 A C ATOM 1166 NZ LYS A 184 15.044 50.618 15.091 1.00 55.97 A N ATOM 1167 C LYS A 184 17.534 56.047 17.381 1.00 39.29 A C ATOM 1168 O LYS A 184 16.788 56.491 18.248 1.00 42.90 A O ATOM 1169 N ASP A 185 17.541 56.476 16.116 1.00 38.95 A N ATOM 1170 CA ASP A 185 16.667 57.545 15.608 1.00 38.91 A C ATOM 1171 CB ASP A 185 15.197 57.098 15.592 1.00 36.81 A C ATOM 1172 CG ASP A 185 14.960 55.913 14.677 1.00 42.98 A C ATOM 1173 OD1 ASP A 185 15.496 55.913 13.542 1.00 39.11 A O ATOM 1174 OD2 ASP A 185 14.238 54.976 15.090 1.00 44.37 A O ATOM 1175 C ASP A 185 16.839 58.873 16.369 1.00 39.84 A C ATOM 1176 O ASP A 185 17.775 59.041 17.140 1.00 36.15 A O ATOM 1177 N GLY A 186 15.932 59.820 16.156 1.00 33.09 A N ATOM 1178 CA GLY A 186 16.137 61.144 16.728 1.00 38.52 A C ATOM 1179 C GLY A 186 17.212 61.922 15.966 1.00 33.48 A C ATOM 1180 O GLY A 186 17.092 62.088 14.756 1.00 30.67 A O ATOM 1181 N LEU A 187 18.218 62.421 16.687 1.00 34.59 A N ATOM 1182 CA LEU A 187 19.400 63.060 16.101 1.00 38.17 A C ATOM 1183 CB LEU A 187 20.355 63.500 17.203 1.00 33.91 A C ATOM 1184 CG LEU A 187 20.162 64.847 17.868 1.00 38.96 A C ATOM 1185 CD1 LEU A 187 18.693 65.047 18.200 1.00 42.27 A C ATOM 1186 CD2 LEU A 187 21.002 64.888 19.112 1.00 34.78 A C ATOM 1187 C LEU A 187 20.177 62.065 15.265 1.00 36.34 A C ATOM 1188 O LEU A 187 20.555 61.030 15.771 1.00 33.51 A O ATOM 1189 N LEU A 188 20.451 62.376 14.005 1.00 32.50 A N ATOM 1190 CA LEU A 188 21.205 61.447 13.174 1.00 31.84 A C ATOM 1191 CB LEU A 188 20.681 61.488 11.751 1.00 26.47 A C ATOM 1192 CG LEU A 188 19.221 61.053 11.629 1.00 26.96 A C ATOM 1193 CD1 LEU A 188 18.818 60.983 10.193 1.00 23.19 A C ATOM 1194 CD2 LEU A 188 19.012 59.710 12.340 1.00 30.11 A C ATOM 1195 C LEU A 188 22.730 61.679 13.192 1.00 36.14 A C ATOM 1196 O LEU A 188 23.502 60.736 13.011 1.00 32.78 A O ATOM 1197 N ALA A 189 23.147 62.915 13.445 1.00 34.06 A N ATOM 1198 CA ALA A 189 24.527 63.333 13.214 1.00 32.49 A C ATOM 1199 CB ALA A 189 24.919 63.008 11.803 1.00 30.03 A C ATOM 1200 C ALA A 189 24.676 64.824 13.416 1.00 35.57 A C ATOM 1201 O ALA A 189 23.695 65.557 13.455 1.00 32.73 A O ATOM 1202 N HIS A 190 25.913 65.290 13.504 1.00 35.42 A N ATOM 1203 CA HIS A 190 26.139 66.722 13.499 1.00 30.33 A C ATOM 1204 CB HIS A 190 25.971 67.285 14.892 1.00 31.73 A C ATOM 1205 CG HIS A 190 26.809 66.600 15.913 1.00 36.95 A C ATOM 1206 CD2 HIS A 190 28.070 66.114 15.844 1.00 36.72 A C ATOM 1207 ND1 HIS A 190 26.364 66.342 17.193 1.00 37.81 A N ATOM 1208 CE1 HIS A 190 27.323 65.734 17.871 1.00 38.27 A C ATOM 1209 NE2 HIS A 190 28.365 65.580 17.074 1.00 32.13 A N ATOM 1210 C HIS A 190 27.521 67.106 12.988 1.00 38.91 A C ATOM 1211 O HIS A 190 28.369 66.249 12.702 1.00 29.31 A O ATOM 1212 N ALA A 191 27.749 68.413 12.924 1.00 36.50 A N ATOM 1213 CA ALA A 191 28.993 68.928 12.384 1.00 35.36 A C ATOM 1214 CB ALA A 191 28.998 68.798 10.881 1.00 23.07 A C ATOM 1215 C ALA A 191 29.145 70.383 12.789 1.00 39.61 A C ATOM 1216 O ALA A 191 28.152 71.089 13.042 1.00 31.75 A O ATOM 1217 N PHE A 192 30.397 70.817 12.827 1.00 29.58 A N ATOM 1218 CA PHE A 192 30.746 72.145 13.282 1.00 32.07 A C ATOM 1219 CB PHE A 192 31.792 72.020 14.370 1.00 35.62 A C ATOM 1220 CG PHE A 192 31.467 70.987 15.418 1.00 37.98 A C ATOM 1221 CD1 PHE A 192 31.230 71.365 16.726 1.00 37.11 A C ATOM 1222 CD2 PHE A 192 31.407 69.645 15.095 1.00 39.76 A C ATOM 1223 CE1 PHE A 192 30.953 70.427 17.695 1.00 40.37 A C ATOM 1224 CE2 PHE A 192 31.121 68.701 16.060 1.00 40.71 A C ATOM 1225 CZ PHE A 192 30.893 69.096 17.364 1.00 41.36 A C ATOM 1226 C PHE A 192 31.275 73.005 12.123 1.00 35.65 A C ATOM 1227 O PHE A 192 31.880 72.497 11.183 1.00 36.24 A O ATOM 1228 N PRO A 193 31.055 74.318 12.201 1.00 34.67 A N ATOM 1229 CD PRO A 193 30.590 75.020 13.407 1.00 28.79 A C ATOM 1230 CA PRO A 193 31.405 75.248 11.119 1.00 34.65 A C ATOM 1231 CB PRO A 193 30.917 76.588 11.653 1.00 29.53 A C ATOM 1232 CG PRO A 193 31.085 76.424 13.169 1.00 36.90 A C ATOM 1233 C PRO A 193 32.917 75.323 10.977 1.00 34.52 A C ATOM 1234 O PRO A 193 33.626 74.953 11.913 1.00 35.07 A O ATOM 1235 N PRO A 194 33.397 75.830 9.830 1.00 36.03 A N ATOM 1236 CD PRO A 194 32.537 76.202 8.694 1.00 33.20 A C ATOM 1237 CA PRO A 194 34.824 76.001 9.515 1.00 35.65 A C ATOM 1238 CB PRO A 194 34.796 76.934 8.301 1.00 35.65 A C ATOM 1239 CG PRO A 194 33.539 76.550 7.587 1.00 33.79 A C ATOM 1240 C PRO A 194 35.630 76.636 10.638 1.00 33.22 A C ATOM 1241 O PRO A 194 35.173 77.568 11.284 1.00 32.62 A O ATOM 1242 N GLY A 195 36.840 76.129 10.853 1.00 38.40 A N ATOM 1243 CA GLY A 195 37.747 76.714 11.824 1.00 34.27 A C ATOM 1244 C GLY A 195 38.769 75.741 12.376 1.00 32.87 A C ATOM 1245 O GLY A 195 38.941 74.647 11.859 1.00 35.51 A O ATOM 1246 N PRO A 196 39.436 76.141 13.459 1.00 32.51 A N ATOM 1247 CD PRO A 196 39.236 77.495 13.985 1.00 33.53 A C ATOM 1248 CA PRO A 196 40.449 75.395 14.213 1.00 37.94 A C ATOM 1249 CB PRO A 196 40.942 76.414 15.250 1.00 34.07 A C ATOM 1250 CG PRO A 196 40.468 77.721 14.790 1.00 41.17 A C ATOM 1251 C PRO A 196 39.869 74.214 14.971 1.00 43.64 A C ATOM 1252 O PRO A 196 38.754 74.283 15.500 1.00 43.08 A O ATOM 1253 N GLY A 197 40.644 73.143 15.041 1.00 39.76 A N ATOM 1254 CA GLY A 197 40.365 72.059 15.948 1.00 40.08 A C ATOM 1255 C GLY A 197 39.195 71.201 15.537 1.00 46.40 A C ATOM 1256 O GLY A 197 39.235 70.531 14.514 1.00 42.59 A O ATOM 1257 N ILE A 198 38.151 71.226 16.356 1.00 42.14 A N ATOM 1258 CA ILE A 198 36.975 70.405 16.144 1.00 42.92 A C ATOM 1259 CB ILE A 198 36.202 70.233 17.468 1.00 42.35 A C ATOM 1260 CG2 ILE A 198 35.684 71.602 17.982 1.00 34.79 A C ATOM 1261 CG1 ILE A 198 35.075 69.223 17.285 1.00 41.12 A C ATOM 1262 CD1 ILE A 198 34.456 68.762 18.592 1.00 46.02 A C ATOM 1263 C ILE A 198 36.092 71.049 15.080 1.00 37.02 A C ATOM 1264 O ILE A 198 35.412 70.373 14.300 1.00 39.58 A O ATOM 1265 N GLN A 199 36.120 72.368 15.032 1.00 35.42 A N ATOM 1266 CA GLN A 199 35.398 73.060 13.991 1.00 36.83 A C ATOM 1267 CB GLN A 199 35.748 74.545 14.011 1.00 36.87 A C ATOM 1268 CG GLN A 199 35.308 75.195 15.313 1.00 37.86 A C ATOM 1269 CD GLN A 199 35.548 76.681 15.363 1.00 36.36 A C ATOM 1270 OE1 GLN A 199 35.268 77.405 14.407 1.00 37.90 A O ATOM 1271 NE2 GLN A 199 36.079 77.146 16.486 1.00 36.32 A N ATOM 1272 C GLN A 199 35.709 72.419 12.647 1.00 40.12 A C ATOM 1273 O GLN A 199 36.845 72.070 12.371 1.00 37.82 A O ATOM 1274 N GLY A 200 34.687 72.257 11.817 1.00 35.22 A N ATOM 1275 CA GLY A 200 34.839 71.574 10.558 1.00 27.82 A C ATOM 1276 C GLY A 200 34.533 70.086 10.690 1.00 28.02 A C ATOM 1277 O GLY A 200 34.218 69.431 9.701 1.00 28.40 A O ATOM 1278 N ASP A 201 34.639 69.536 11.892 1.00 27.66 A N ATOM 1279 CA ASP A 201 34.435 68.083 12.050 1.00 31.79 A C ATOM 1280 CB ASP A 201 34.969 67.605 13.392 1.00 31.24 A C ATOM 1281 CG ASP A 201 36.476 67.611 13.438 1.00 36.87 A C ATOM 1282 OD1 ASP A 201 37.093 67.990 12.411 1.00 33.76 A O ATOM 1283 OD2 ASP A 201 37.030 67.248 14.495 1.00 38.77 A O ATOM 1284 C ASP A 201 32.986 67.619 11.872 1.00 29.98 A C ATOM 1285 O ASP A 201 32.056 68.397 12.082 1.00 27.07 A O ATOM 1286 N ALA A 202 32.818 66.359 11.477 1.00 28.93 A N ATOM 1287 CA ALA A 202 31.506 65.788 11.207 1.00 33.46 A C ATOM 1288 CB ALA A 202 31.284 65.693 9.706 1.00 31.07 A C ATOM 1289 C ALA A 202 31.300 64.409 11.858 1.00 35.35 A C ATOM 1290 O ALA A 202 31.980 63.444 11.508 1.00 33.67 A O ATOM 1291 N HIS A 203 30.335 64.311 12.771 1.00 33.44 A N ATOM 1292 CA HIS A 203 30.049 63.053 13.472 1.00 31.74 A C ATOM 1293 CB HIS A 203 30.147 63.297 14.961 1.00 33.03 A C ATOM 1294 CG HIS A 203 31.434 63.930 15.356 1.00 36.44 A C ATOM 1295 CD2 HIS A 203 32.677 63.805 14.840 1.00 34.93 A C ATOM 1296 ND1 HIS A 203 31.533 64.856 16.366 1.00 39.90 A N ATOM 1297 CE1 HIS A 203 32.782 65.264 16.476 1.00 39.48 A C ATOM 1298 NE2 HIS A 203 33.499 64.643 15.556 1.00 41.70 A N ATOM 1299 C HIS A 203 28.710 62.387 13.116 1.00 33.98 A C ATOM 1300 O HIS A 203 27.680 63.067 12.998 1.00 32.83 A O ATOM 1301 N PHE A 204 28.744 61.066 12.944 1.00 30.19 A N ATOM 1302 CA PHE A 204 27.564 60.268 12.598 1.00 32.67 A C ATOM 1303 CB PHE A 204 27.809 59.505 11.309 1.00 31.59 A C ATOM 1304 CG PHE A 204 28.164 60.390 10.182 1.00 35.12 A C ATOM 1305 CD1 PHE A 204 29.445 60.869 10.054 1.00 35.13 A C ATOM 1306 CD2 PHE A 204 27.201 60.815 9.293 1.00 31.17 A C ATOM 1307 CE1 PHE A 204 29.764 61.726 9.022 1.00 35.15 A C ATOM 1308 CE2 PHE A 204 27.514 61.656 8.261 1.00 29.77 A C ATOM 1309 CZ PHE A 204 28.799 62.121 8.129 1.00 26.50 A C ATOM 1310 C PHE A 204 27.188 59.274 13.673 1.00 33.67 A C ATOM 1311 O PHE A 204 28.047 58.546 14.170 1.00 33.13 A O ATOM 1312 N ASP A 205 25.894 59.225 14.005 1.00 36.16 A N ATOM 1313 CA ASP A 205 25.402 58.386 15.093 1.00 32.51 A C ATOM 1314 CB ASP A 205 24.018 58.829 15.599 1.00 36.04 A C ATOM 1315 CG ASP A 205 23.601 58.077 16.888 1.00 38.97 A C ATOM 1316 OD1 ASP A 205 24.142 56.984 17.143 1.00 36.43 A O ATOM 1317 OD2 ASP A 205 22.767 58.585 17.665 1.00 38.39 A O ATOM 1318 C ASP A 205 25.320 56.934 14.679 1.00 31.72 A C ATOM 1319 O ASP A 205 24.396 56.529 13.962 1.00 30.03 A O ATOM 1320 N ASP A 206 26.268 56.145 15.180 1.00 35.43 A N ATOM 1321 CA ASP A 206 26.377 54.755 14.788 1.00 34.03 A C ATOM 1322 CB ASP A 206 27.797 54.256 15.016 1.00 36.16 A C ATOM 1323 CG ASP A 206 28.116 53.005 14.217 1.00 26.64 A C ATOM 1324 OD1 ASP A 206 27.469 52.714 13.181 1.00 23.12 A O ATOM 1325 OD2 ASP A 206 29.046 52.297 14.651 1.00 40.86 A O ATOM 1326 C ASP A 206 25.354 53.857 15.485 1.00 36.31 A C ATOM 1327 O ASP A 206 25.307 52.659 15.219 1.00 32.06 A O ATOM 1328 N ASP A 207 24.536 54.437 16.363 1.00 35.09 A N ATOM 1329 CA ASP A 207 23.346 53.743 16.855 1.00 36.67 A C ATOM 1330 CB ASP A 207 22.799 54.358 18.157 1.00 35.77 A C ATOM 1331 CG ASP A 207 23.528 53.849 19.404 1.00 35.38 A C ATOM 1332 OD1 ASP A 207 24.025 52.703 19.379 1.00 35.82 A O ATOM 1333 OD2 ASP A 207 23.627 54.593 20.405 1.00 32.10 A O ATOM 1334 C ASP A 207 22.282 53.739 15.766 1.00 35.79 A C ATOM 1335 O ASP A 207 21.238 53.130 15.926 1.00 40.02 A O ATOM 1336 N GLU A 208 22.543 54.405 14.645 1.00 35.25 A N ATOM 1337 CA GLU A 208 21.662 54.279 13.485 1.00 29.68 A C ATOM 1338 CB GLU A 208 21.591 55.586 12.691 1.00 28.98 A C ATOM 1339 CG GLU A 208 21.392 56.837 13.512 1.00 35.67 A C ATOM 1340 CD GLU A 208 20.029 56.876 14.166 1.00 39.48 A C ATOM 1341 OE1 GLU A 208 19.170 56.020 13.826 1.00 31.07 A O ATOM 1342 OE2 GLU A 208 19.832 57.765 15.016 1.00 35.43 A O ATOM 1343 C GLU A 208 22.150 53.202 12.532 1.00 31.79 A C ATOM 1344 O GLU A 208 23.352 52.965 12.428 1.00 35.08 A O ATOM 1345 N LEU A 209 21.230 52.582 11.796 1.00 28.93 A N ATOM 1346 CA LEU A 209 21.631 51.659 10.746 1.00 31.71 A C ATOM 1347 CB LEU A 209 20.506 50.694 10.361 1.00 31.99 A C ATOM 1348 CG LEU A 209 20.775 49.672 9.251 1.00 31.34 A C ATOM 1349 CD1 LEU A 209 21.734 48.596 9.748 1.00 29.47 A C ATOM 1350 CD2 LEU A 209 19.476 49.047 8.731 1.00 32.60 A C ATOM 1351 C LEU A 209 22.003 52.513 9.540 1.00 34.45 A C ATOM 1352 O LEU A 209 21.140 53.157 8.930 1.00 31.60 A O ATOM 1353 N TRP A 210 23.287 52.520 9.191 1.00 32.56 A N ATOM 1354 CA TRP A 210 23.704 53.276 8.017 1.00 32.42 A C ATOM 1355 CB TRP A 210 25.112 53.848 8.222 1.00 29.33 A C ATOM 1356 CG TRP A 210 25.084 54.888 9.277 1.00 22.77 A C ATOM 1357 CD2 TRP A 210 24.497 56.189 9.161 1.00 25.25 A C ATOM 1358 CE2 TRP A 210 24.675 56.840 10.395 1.00 23.41 A C ATOM 1359 CE3 TRP A 210 23.844 56.871 8.122 1.00 30.29 A C ATOM 1360 CD1 TRP A 210 25.558 54.794 10.538 1.00 26.47 A C ATOM 1361 NE1 TRP A 210 25.343 55.973 11.220 1.00 22.82 A N ATOM 1362 CZ2 TRP A 210 24.214 58.140 10.630 1.00 25.61 A C ATOM 1363 CZ3 TRP A 210 23.393 58.174 8.355 1.00 20.72 A C ATOM 1364 CH2 TRP A 210 23.591 58.791 9.594 1.00 20.72 A C ATOM 1365 C TRP A 210 23.561 52.436 6.758 1.00 32.67 A C ATOM 1366 O TRP A 210 23.914 51.259 6.743 1.00 32.77 A O ATOM 1367 N SER A 211 22.992 53.029 5.716 1.00 28.60 A N ATOM 1368 CA SER A 211 22.938 52.355 4.435 1.00 29.73 A C ATOM 1369 CB SER A 211 21.654 51.543 4.292 1.00 38.84 A C ATOM 1370 OG SER A 211 20.525 52.400 4.178 1.00 39.82 A O ATOM 1371 C SER A 211 23.032 53.379 3.321 1.00 28.13 A C ATOM 1372 O SER A 211 23.526 54.492 3.497 1.00 28.42 A O ATOM 1373 N LEU A 212 22.563 52.999 2.155 1.00 31.48 A N ATOM 1374 CA LEU A 212 22.514 53.948 1.064 1.00 36.59 A C ATOM 1375 CB LEU A 212 23.375 53.474 −0.096 1.00 34.16 A C ATOM 1376 CG LEU A 212 24.639 54.293 −0.316 1.00 31.22 A C ATOM 1377 CD1 LEU A 212 25.570 54.141 0.846 1.00 29.54 A C ATOM 1378 CD2 LEU A 212 25.288 53.830 −1.610 1.00 35.76 A C ATOM 1379 C LEU A 212 21.087 54.012 0.617 1.00 42.23 A C ATOM 1380 O LEU A 212 20.593 55.052 0.187 1.00 39.67 A O ATOM 1381 N GLY A 213 20.433 52.863 0.739 1.00 51.39 A N ATOM 1382 CA GLY A 213 19.085 52.684 0.248 1.00 55.69 A C ATOM 1383 C GLY A 213 18.026 53.456 1.007 1.00 50.21 A C ATOM 1384 O GLY A 213 18.341 54.297 1.860 1.00 47.17 A O ATOM 1385 N LYS A 389 16.766 53.134 0.730 1.00 54.86 A N ATOM 1386 CA LYS A 389 16.398 51.955 −0.074 1.00 54.61 A C ATOM 1387 CB LYS A 389 16.965 51.991 −1.499 1.00 52.87 A C ATOM 1388 CG LYS A 389 16.496 53.187 −2.314 1.00 55.29 A C ATOM 1389 CD LYS A 389 15.000 53.120 −2.662 1.00 59.26 A C ATOM 1390 CE LYS A 389 14.740 52.274 −3.919 1.00 60.06 A C ATOM 1391 NZ LYS A 389 13.600 52.802 −4.749 1.00 56.51 A N ATOM 1392 C LYS A 389 16.750 50.645 0.631 1.00 53.94 A C ATOM 1393 O LYS A 389 17.919 50.367 0.944 1.00 48.23 A O ATOM 1394 N GLY A 390 15.710 49.850 0.866 1.00 49.25 A N ATOM 1395 CA GLY A 390 15.808 48.651 1.668 1.00 47.39 A C ATOM 1396 C GLY A 390 15.520 49.014 3.110 1.00 50.25 A C ATOM 1397 O GLY A 390 14.370 48.983 3.556 1.00 57.97 A O ATOM 1398 N GLN A 391 16.568 49.368 3.837 1.00 43.28 A N ATOM 1399 CA GLN A 391 16.443 49.761 5.223 1.00 40.21 A C ATOM 1400 CB GLN A 391 16.492 48.523 6.116 1.00 39.87 A C ATOM 1401 CG GLN A 391 15.254 47.615 5.924 1.00 44.25 A C ATOM 1402 CD GLN A 391 15.387 46.217 6.520 1.00 38.26 A C ATOM 1403 OE1 GLN A 391 15.910 46.035 7.622 1.00 40.73 A O ATOM 1404 NE2 GLN A 391 14.886 45.222 5.793 1.00 36.24 A N ATOM 1405 C GLN A 391 17.576 50.733 5.529 1.00 44.73 A C ATOM 1406 O GLN A 391 18.493 50.883 4.724 1.00 42.29 A O ATOM 1407 N GLY A 392 17.492 51.408 6.672 1.00 38.28 A N ATOM 1408 CA GLY A 392 18.540 52.297 7.128 1.00 30.99 A C ATOM 1409 C GLY A 392 18.477 53.662 6.481 1.00 36.64 A C ATOM 1410 O GLY A 392 17.744 53.871 5.509 1.00 34.19 A O ATOM 1411 N TYR A 393 19.260 54.587 7.032 1.00 37.67 A N ATOM 1412 CA TYR A 393 19.424 55.938 6.496 1.00 32.31 A C ATOM 1413 CB TYR A 393 19.722 56.900 7.641 1.00 30.99 A C ATOM 1414 CG TYR A 393 18.624 57.051 8.665 1.00 35.37 A C ATOM 1415 CD1 TYR A 393 17.525 57.869 8.413 1.00 34.11 A C ATOM 1416 CE1 TYR A 393 16.516 58.024 9.345 1.00 30.74 A C ATOM 1417 CD2 TYR A 393 18.696 56.399 9.895 1.00 35.46 A C ATOM 1418 CE2 TYR A 393 17.693 56.544 10.827 1.00 40.89 A C ATOM 1419 CZ TYR A 393 16.605 57.365 10.538 1.00 35.37 A C ATOM 1420 OH TYR A 393 15.609 57.526 11.454 1.00 40.33 A O ATOM 1421 C TYR A 393 20.602 56.036 5.507 1.00 33.64 A C ATOM 1422 O TYR A 393 21.625 55.397 5.695 1.00 31.02 A O ATOM 1423 N SER A 394 20.468 56.886 4.497 1.00 33.38 A N ATOM 1424 CA SER A 394 21.518 57.085 3.493 1.00 28.60 A C ATOM 1425 CB SER A 394 20.922 57.763 2.247 1.00 31.01 A C ATOM 1426 OG SER A 394 21.873 58.076 1.240 1.00 34.83 A O ATOM 1427 C SER A 394 22.697 57.887 4.046 1.00 28.77 A C ATOM 1428 O SER A 394 22.601 59.102 4.273 1.00 25.83 A O ATOM 1429 N LEU A 395 23.817 57.204 4.268 1.00 25.99 A N ATOM 1430 CA LEU A 395 25.051 57.898 4.616 1.00 30.77 A C ATOM 1431 CB LEU A 395 26.198 56.908 4.711 1.00 27.36 A C ATOM 1432 CG LEU A 395 27.474 57.436 5.354 1.00 29.25 A C ATOM 1433 CD1 LEU A 395 27.182 57.916 6.750 1.00 26.12 A C ATOM 1434 CD2 LEU A 395 28.534 56.341 5.363 1.00 23.17 A C ATOM 1435 C LEU A 395 25.391 58.989 3.598 1.00 23.86 A C ATOM 1436 O LEU A 395 25.801 60.080 3.953 1.00 31.47 A O ATOM 1437 N PHE A 396 25.198 58.687 2.331 1.00 24.58 A N ATOM 1438 CA PHE A 396 25.489 59.641 1.286 1.00 25.13 A C ATOM 1439 CB PHE A 396 25.078 59.066 −0.073 1.00 24.32 A C ATOM 1440 CG PHE A 396 25.174 60.051 −1.201 1.00 26.86 A C ATOM 1441 CD1 PHE A 396 26.310 60.862 −1.346 1.00 29.65 A C ATOM 1442 CD2 PHE A 396 24.145 60.182 −2.107 1.00 25.09 A C ATOM 1443 CE1 PHE A 396 26.409 61.786 −2.379 1.00 21.52 A C ATOM 1444 CE2 PHE A 396 24.232 61.115 −3.161 1.00 33.69 A C ATOM 1445 CZ PHE A 396 25.377 61.913 −3.293 1.00 25.00 A C ATOM 1446 C PHE A 396 24.785 60.965 1.583 1.00 31.10 A C ATOM 1447 O PHE A 396 25.441 62.006 1.745 1.00 25.39 A O ATOM 1448 N LEU A 397 23.451 60.900 1.695 1.00 30.63 A N ATOM 1449 CA LEU A 397 22.595 62.077 1.905 1.00 28.84 A C ATOM 1450 CB LEU A 397 21.129 61.659 1.931 1.00 24.21 A C ATOM 1451 CG LEU A 397 20.585 61.350 0.541 1.00 23.84 A C ATOM 1452 CD1 LEU A 397 19.133 60.974 0.579 1.00 30.42 A C ATOM 1453 CD2 LEU A 397 20.776 62.580 −0.331 1.00 29.27 A C ATOM 1454 C LEU A 397 22.920 62.857 3.158 1.00 24.45 A C ATOM 1455 O LEU A 397 23.092 64.072 3.106 1.00 25.25 A O ATOM 1456 N VAL A 398 22.992 62.153 4.281 1.00 19.58 A N ATOM 1457 CA VAL A 398 23.326 62.757 5.556 1.00 22.66 A C ATOM 1458 CB VAL A 398 23.299 61.671 6.684 1.00 25.46 A C ATOM 1459 CG1 VAL A 398 23.830 62.221 7.961 1.00 27.06 A C ATOM 1460 CG2 VAL A 398 21.865 61.127 6.893 1.00 28.73 A C ATOM 1461 C VAL A 398 24.707 63.460 5.507 1.00 29.30 A C ATOM 1462 O VAL A 398 24.853 64.619 5.938 1.00 26.62 A O ATOM 1463 N ALA A 399 25.718 62.743 5.004 1.00 27.68 A N ATOM 1464 CA ALA A 399 27.063 63.318 4.832 1.00 28.70 A C ATOM 1465 CB ALA A 399 28.030 62.290 4.141 1.00 23.22 A C ATOM 1466 C ALA A 399 27.013 64.626 4.040 1.00 19.96 A C ATOM 1467 O ALA A 399 27.534 65.656 4.470 1.00 26.15 A O ATOM 1468 N ALA A 400 26.376 64.600 2.889 1.00 25.46 A N ATOM 1469 CA ALA A 400 26.204 65.834 2.118 1.00 21.78 A C ATOM 1470 CB ALA A 400 25.315 65.589 0.941 1.00 20.42 A C ATOM 1471 C ALA A 400 25.682 66.994 2.977 1.00 31.85 A C ATOM 1472 O ALA A 400 26.222 68.135 2.931 1.00 26.53 A O ATOM 1473 N HIS A 401 24.644 66.714 3.770 1.00 25.59 A N ATOM 1474 CA HIS A 401 24.075 67.746 4.636 1.00 26.62 A C ATOM 1475 CB HIS A 401 22.848 67.184 5.388 1.00 29.73 A C ATOM 1476 CG HIS A 401 22.241 68.139 6.367 1.00 23.42 A C ATOM 1477 CD2 HIS A 401 22.577 68.460 7.638 1.00 24.84 A C ATOM 1478 ND1 HIS A 401 21.121 68.886 6.069 1.00 24.58 A N ATOM 1479 CE1 HIS A 401 20.809 69.645 7.103 1.00 22.83 A C ATOM 1480 NE2 HIS A 401 21.666 69.400 8.078 1.00 18.99 A N ATOM 1481 C HIS A 401 25.113 68.239 5.621 1.00 22.18 A C ATOM 1482 O HIS A 401 25.348 69.446 5.760 1.00 22.06 A O ATOM 1483 N GLU A 402 25.731 67.311 6.339 1.00 24.84 A N ATOM 1484 CA GLU A 402 26.715 67.688 7.357 1.00 24.15 A C ATOM 1485 CB GLU A 402 27.140 66.479 8.191 1.00 26.68 A C ATOM 1486 CG GLU A 402 25.987 65.731 8.880 1.00 30.49 A C ATOM 1487 CD GLU A 402 25.229 66.577 9.878 1.00 29.67 A C ATOM 1488 OE1 GLU A 402 25.813 67.511 10.469 1.00 27.32 A O ATOM 1489 OE2 GLU A 402 24.025 66.294 10.077 1.00 35.89 A O ATOM 1490 C GLU A 402 27.985 68.348 6.783 1.00 24.01 A C ATOM 1491 O GLU A 402 28.619 69.151 7.461 1.00 25.88 A O ATOM 1492 N PHE A 403 28.373 68.001 5.560 1.00 27.66 A N ATOM 1493 CA PHE A 403 29.558 68.652 4.952 1.00 27.50 A C ATOM 1494 CB PHE A 403 30.005 67.930 3.674 1.00 22.21 A C ATOM 1495 CG PHE A 403 30.550 66.553 3.923 1.00 24.05 A C ATOM 1496 CD1 PHE A 403 30.907 66.163 5.206 1.00 28.46 A C ATOM 1497 CD2 PHE A 403 30.689 65.637 2.883 1.00 23.98 A C ATOM 1498 CE1 PHE A 403 31.382 64.868 5.456 1.00 24.96 A C ATOM 1499 CE2 PHE A 403 31.173 64.375 3.109 1.00 25.01 A C ATOM 1500 CZ PHE A 403 31.516 63.975 4.401 1.00 24.31 A C ATOM 1501 C PHE A 403 29.176 70.101 4.682 1.00 27.96 A C ATOM 1502 O PHE A 403 30.003 71.016 4.754 1.00 29.09 A O ATOM 1503 N GLY A 404 27.881 70.316 4.447 1.00 26.82 A N ATOM 1504 CA GLY A 404 27.366 71.661 4.249 1.00 19.60 A C ATOM 1505 C GLY A 404 27.593 72.578 5.428 1.00 20.79 A C ATOM 1506 O GLY A 404 27.812 73.788 5.256 1.00 27.69 A O ATOM 1507 N HIS A 405 27.515 72.026 6.629 1.00 23.53 A N ATOM 1508 CA HIS A 405 27.797 72.790 7.826 1.00 22.68 A C ATOM 1509 CB HIS A 405 27.340 72.040 9.091 1.00 26.79 A C ATOM 1510 CG HIS A 405 25.855 72.039 9.289 1.00 25.71 A C ATOM 1511 CD2 HIS A 405 24.988 71.027 9.523 1.00 23.80 A C ATOM 1512 ND1 HIS A 405 25.096 73.188 9.204 1.00 22.22 A N ATOM 1513 CE1 HIS A 405 23.821 72.885 9.398 1.00 29.49 A C ATOM 1514 NE2 HIS A 405 23.730 71.585 9.603 1.00 32.20 A N ATOM 1515 C HIS A 405 29.312 72.973 7.912 1.00 29.63 A C ATOM 1516 O HIS A 405 29.802 74.010 8.385 1.00 26.07 A O ATOM 1517 N ALA A 406 30.043 71.941 7.491 1.00 25.67 A N ATOM 1518 CA ALA A 406 31.509 71.945 7.627 1.00 29.10 A C ATOM 1519 CB ALA A 406 32.078 70.586 7.263 1.00 25.62 A C ATOM 1520 C ALA A 406 32.138 73.048 6.761 1.00 25.23 A C ATOM 1521 O ALA A 406 33.258 73.477 7.010 1.00 33.63 A O ATOM 1522 N LEU A 407 31.410 73.465 5.731 1.00 24.80 A N ATOM 1523 CA LEU A 407 31.804 74.571 4.882 1.00 24.81 A C ATOM 1524 CB LEU A 407 31.395 74.288 3.451 1.00 18.80 A C ATOM 1525 CG LEU A 407 31.986 72.990 2.914 1.00 25.53 A C ATOM 1526 CD1 LEU A 407 31.496 72.729 1.515 1.00 23.35 A C ATOM 1527 CD2 LEU A 407 33.526 73.038 2.982 1.00 22.56 A C ATOM 1528 C LEU A 407 31.223 75.903 5.296 1.00 31.44 A C ATOM 1529 O LEU A 407 31.529 76.915 4.667 1.00 33.50 A O ATOM 1530 N GLY A 408 30.370 75.908 6.326 1.00 32.79 A N ATOM 1531 CA GLY A 408 29.819 77.141 6.860 1.00 24.97 A C ATOM 1532 C GLY A 408 28.334 77.401 6.585 1.00 29.02 A C ATOM 1533 O GLY A 408 27.868 78.536 6.742 1.00 28.57 A O ATOM 1534 N LEU A 409 27.584 76.386 6.163 1.00 26.49 A N ATOM 1535 CA LEU A 409 26.151 76.596 5.877 1.00 28.63 A C ATOM 1536 CB LEU A 409 25.648 75.717 4.739 1.00 25.88 A C ATOM 1537 CG LEU A 409 26.179 76.061 3.336 1.00 22.16 A C ATOM 1538 CD1 LEU A 409 25.633 75.138 2.283 1.00 23.06 A C ATOM 1539 CD2 LEU A 409 25.860 77.517 2.974 1.00 24.52 A C ATOM 1540 C LEU A 409 25.303 76.379 7.126 1.00 29.23 A C ATOM 1541 O LEU A 409 25.674 75.614 8.015 1.00 27.90 A O ATOM 1542 N ASP A 410 24.183 77.095 7.194 1.00 36.70 A N ATOM 1543 CA ASP A 410 23.198 76.915 8.254 1.00 31.57 A C ATOM 1544 CB ASP A 410 22.749 78.251 8.783 1.00 28.53 A C ATOM 1545 CG ASP A 410 23.745 78.849 9.676 1.00 27.81 A C ATOM 1546 OD1 ASP A 410 24.355 78.089 10.436 1.00 41.70 A O ATOM 1547 OD2 ASP A 410 23.948 80.074 9.607 1.00 37.66 A O ATOM 1548 C ASP A 410 22.008 76.209 7.684 1.00 33.29 A C ATOM 1549 O ASP A 410 21.877 76.097 6.466 1.00 29.05 A O ATOM 1550 N HIS A 411 21.121 75.739 8.562 1.00 33.49 A N ATOM 1551 CA HIS A 411 19.932 75.035 8.101 1.00 23.48 A C ATOM 1552 CB HIS A 411 19.083 74.557 9.287 1.00 30.65 A C ATOM 1553 CG HIS A 411 19.674 73.383 9.993 1.00 27.07 A C ATOM 1554 CD2 HIS A 411 20.241 72.251 9.513 1.00 22.87 A C ATOM 1555 ND1 HIS A 411 19.781 73.313 11.367 1.00 29.80 A N ATOM 1556 CE1 HIS A 411 20.361 72.175 11.703 1.00 29.66 A C ATOM 1557 NE2 HIS A 411 20.650 71.515 10.595 1.00 31.14 A N ATOM 1558 C HIS A 411 19.128 75.925 7.199 1.00 19.82 A C ATOM 1559 O HIS A 411 19.108 77.131 7.361 1.00 24.63 A O ATOM 1560 N SER A 412 18.476 75.320 6.226 1.00 19.96 A N ATOM 1561 CA SER A 412 17.523 76.048 5.422 1.00 26.83 A C ATOM 1562 CB SER A 412 17.551 75.513 4.012 1.00 19.72 A C ATOM 1563 OG SER A 412 16.523 76.112 3.263 1.00 22.68 A O ATOM 1564 C SER A 412 16.117 75.838 5.968 1.00 26.56 A C ATOM 1565 O SER A 412 15.877 74.859 6.642 1.00 25.38 A O ATOM 1566 N SER A 413 15.208 76.745 5.626 1.00 28.86 A N ATOM 1567 CA SER A 413 13.780 76.632 5.964 1.00 34.11 A C ATOM 1568 CB SER A 413 13.229 77.980 6.420 1.00 28.72 A C ATOM 1569 OG SER A 413 12.765 78.659 5.271 1.00 38.32 A O ATOM 1570 C SER A 413 12.957 76.166 4.759 1.00 36.22 A C ATOM 1571 O SER A 413 11.745 75.950 4.876 1.00 34.33 A O ATOM 1572 N VAL A 414 13.596 76.040 3.591 1.00 29.78 A N ATOM 1573 CA VAL A 414 12.951 75.389 2.461 1.00 28.33 A C ATOM 1574 CB VAL A 414 13.719 75.631 1.172 1.00 32.14 A C ATOM 1575 CG1 VAL A 414 13.049 74.936 0.005 1.00 29.14 A C ATOM 1576 CG2 VAL A 414 13.844 77.126 0.909 1.00 32.06 A C ATOM 1577 C VAL A 414 12.992 73.896 2.719 1.00 36.80 A C ATOM 1578 O VAL A 414 14.080 73.331 2.783 1.00 34.84 A O ATOM 1579 N PRO A 415 11.819 73.242 2.852 1.00 30.94 A N ATOM 1580 CD PRO A 415 10.483 73.813 2.638 1.00 35.81 A C ATOM 1581 CA PRO A 415 11.745 71.807 3.187 1.00 36.51 A C ATOM 1582 CB PRO A 415 10.228 71.535 3.238 1.00 36.93 A C ATOM 1583 CG PRO A 415 9.599 72.878 3.403 1.00 35.86 A C ATOM 1584 C PRO A 415 12.420 70.846 2.171 1.00 31.98 A C ATOM 1585 O PRO A 415 12.896 69.777 2.554 1.00 33.70 A O ATOM 1586 N GLU A 416 12.448 71.208 0.897 1.00 35.67 A N ATOM 1587 CA GLU A 416 13.086 70.350 −0.116 1.00 38.69 A C ATOM 1588 CB GLU A 416 12.481 70.607 −1.502 1.00 37.34 A C ATOM 1589 CG GLU A 416 10.949 70.457 −1.572 1.00 41.72 A C ATOM 1590 CD GLU A 416 10.188 71.582 −0.866 1.00 43.34 A C ATOM 1591 OE1 GLU A 416 10.452 72.786 −1.118 1.00 35.02 A O ATOM 1592 OE2 GLU A 416 9.298 71.250 −0.056 1.00 53.09 A O ATOM 1593 C GLU A 416 14.626 70.502 −0.167 1.00 36.60 A C ATOM 1594 O GLU A 416 15.341 69.603 −0.615 1.00 36.47 A O ATOM 1595 N ALA A 417 15.122 71.640 0.301 1.00 32.80 A N ATOM 1596 CA ALA A 417 16.557 71.891 0.350 1.00 30.20 A C ATOM 1597 CB ALA A 417 16.844 73.228 1.029 1.00 19.44 A C ATOM 1598 C ALA A 417 17.347 70.773 1.030 1.00 29.68 A C ATOM 1599 O ALA A 417 16.931 70.191 2.021 1.00 26.67 A O ATOM 1600 N LEU A 418 18.537 70.490 0.506 1.00 31.63 A N ATOM 1601 CA LEU A 418 19.458 69.602 1.215 1.00 21.47 A C ATOM 1602 CB LEU A 418 20.747 69.442 0.396 1.00 30.03 A C ATOM 1603 CG LEU A 418 21.841 68.723 1.155 1.00 24.23 A C ATOM 1604 CD1 LEU A 418 21.422 67.275 1.360 1.00 20.16 A C ATOM 1605 CD2 LEU A 418 23.173 68.855 0.361 1.00 25.29 A C ATOM 1606 C LEU A 418 19.809 70.058 2.625 1.00 18.44 A C ATOM 1607 O LEU A 418 20.031 69.237 3.514 1.00 22.59 A O ATOM 1608 N MET A 419 19.899 71.369 2.848 1.00 19.72 A N ATOM 1609 CA MET A 419 20.192 71.870 4.192 1.00 19.83 A C ATOM 1610 CB MET A 419 20.943 73.202 4.118 1.00 24.42 A C ATOM 1611 CG MET A 419 22.409 73.113 3.574 1.00 20.01 A C ATOM 1612 SD MET A 419 23.276 71.676 4.191 1.00 22.60 A S ATOM 1613 CE MET A 419 23.732 72.209 5.816 1.00 22.01 A C ATOM 1614 C MET A 419 18.936 71.992 5.143 1.00 22.22 A C ATOM 1615 O MET A 419 19.042 72.478 6.261 1.00 23.67 A O ATOM 1616 N TYR A 420 17.767 71.542 4.708 1.00 25.58 A N ATOM 1617 CA TYR A 420 16.620 71.464 5.637 1.00 24.58 A C ATOM 1618 CB TYR A 420 15.375 71.015 4.873 1.00 29.53 A C ATOM 1619 CG TYR A 420 14.070 71.212 5.628 1.00 35.10 A C ATOM 1620 CD1 TYR A 420 13.599 72.491 5.918 1.00 34.14 A C ATOM 1621 CE1 TYR A 420 12.390 72.683 6.603 1.00 34.79 A C ATOM 1622 CD2 TYR A 420 13.303 70.113 6.051 1.00 33.62 A C ATOM 1623 CE2 TYR A 420 12.084 70.298 6.741 1.00 34.13 A C ATOM 1624 CZ TYR A 420 11.648 71.583 7.013 1.00 33.50 A C ATOM 1625 OH TYR A 420 10.472 71.783 7.688 1.00 39.71 A O ATOM 1626 C TYR A 420 16.938 70.478 6.758 1.00 25.48 A C ATOM 1627 O TYR A 420 17.379 69.372 6.490 1.00 30.68 A O ATOM 1628 N PRO A 421 16.700 70.858 8.024 1.00 28.89 A N ATOM 1629 CD PRO A 421 15.762 71.916 8.426 1.00 29.11 A C ATOM 1630 CA PRO A 421 17.162 70.052 9.169 1.00 28.03 A C ATOM 1631 CB PRO A 421 16.589 70.785 10.383 1.00 30.37 A C ATOM 1632 CG PRO A 421 16.041 72.091 9.856 1.00 30.64 A C ATOM 1633 C PRO A 421 16.705 68.589 9.220 1.00 27.99 A C ATOM 1634 O PRO A 421 17.445 67.763 9.765 1.00 27.92 A O ATOM 1635 N MET A 422 15.524 68.276 8.694 1.00 24.03 A N ATOM 1636 CA MET A 422 14.961 66.932 8.817 1.00 27.36 A C ATOM 1637 CB MET A 422 13.427 66.256 8.658 1.00 31.70 A C ATOM 1638 CG MET A 422 12.604 67.504 9.835 1.00 35.06 A C ATOM 1639 SD MET A 422 10.821 67.537 9.398 1.00 34.82 A S ATOM 1640 CE MET A 422 10.375 68.997 10.345 1.00 29.02 A C ATOM 1641 C MET A 422 15.464 66.027 7.727 1.00 29.32 A C ATOM 1642 O MET A 422 15.554 66.449 6.574 1.00 30.97 A O ATOM 1643 N TYR A 423 15.728 64.769 8.075 1.00 27.29 A N ATOM 1644 CA TYR A 423 16.030 63.745 7.080 1.00 28.66 A C ATOM 1645 CB TYR A 423 16.412 62.440 7.766 1.00 33.38 A C ATOM 1646 CG TYR A 423 16.768 61.352 6.801 1.00 31.14 A C ATOM 1647 CD1 TYR A 423 15.864 60.353 6.493 1.00 29.67 A C ATOM 1648 CE1 TYR A 423 16.180 59.347 5.604 1.00 34.36 A C ATOM 1649 CD2 TYR A 423 18.030 61.312 6.197 1.00 35.49 A C ATOM 1650 CE2 TYR A 423 18.365 60.300 5.302 1.00 25.95 A C ATOM 1651 CZ TYR A 423 17.442 59.317 5.010 1.00 31.38 A C ATOM 1652 OH TYR A 423 17.741 58.304 4.126 1.00 30.74 A O ATOM 1653 C TYR A 423 14.886 63.448 6.133 1.00 37.85 A C ATOM 1654 O TYR A 423 13.802 63.008 6.568 1.00 38.94 A O ATOM 1655 N ARG A 424 15.138 63.655 4.841 1.00 32.32 A N ATOM 1656 CA ARG A 424 14.224 63.234 3.791 1.00 32.75 A C ATOM 1657 CB ARG A 424 13.659 64.454 3.040 1.00 36.08 A C ATOM 1658 CG ARG A 424 14.396 64.825 1.730 1.00 44.57 A C ATOM 1659 CD ARG A 424 13.728 65.999 1.002 1.00 47.53 A C ATOM 1660 NE ARG A 424 14.210 66.217 −0.368 1.00 45.70 A N ATOM 1661 CZ ARG A 424 13.438 66.149 −1.453 1.00 49.30 A C ATOM 1662 NH1 ARG A 424 12.149 65.853 −1.325 1.00 53.81 A N ATOM 1663 NH2 ARG A 424 13.941 66.370 −2.670 1.00 47.77 A N ATOM 1664 C ARG A 424 15.014 62.372 2.828 1.00 36.90 A C ATOM 1665 O ARG A 424 16.003 62.844 2.254 1.00 43.64 A O ATOM 1666 N PHE A 425 14.621 61.115 2.642 1.00 33.41 A N ATOM 1667 CA PHE A 425 15.268 60.318 1.596 1.00 33.48 A C ATOM 1668 CB PHE A 425 15.102 58.814 1.789 1.00 39.00 A C ATOM 1669 CG PHE A 425 15.660 58.006 0.642 1.00 34.42 A C ATOM 1670 CD1 PHE A 425 17.013 57.735 0.568 1.00 35.68 A C ATOM 1671 CD2 PHE A 425 14.842 57.572 −0.382 1.00 36.21 A C ATOM 1672 CE1 PHE A 425 17.532 57.005 −0.485 1.00 38.14 A C ATOM 1673 CE2 PHE A 425 15.361 56.853 −1.445 1.00 41.73 A C ATOM 1674 CZ PHE A 425 16.707 56.567 −1.489 1.00 36.73 A C ATOM 1675 C PHE A 425 14.760 60.693 0.225 1.00 35.41 A C ATOM 1676 O PHE A 425 13.573 60.923 0.034 1.00 40.53 A O ATOM 1677 N THR A 426 15.673 60.761 −0.735 1.00 33.23 A N ATOM 1678 CA THR A 426 15.332 61.059 −2.119 1.00 34.43 A C ATOM 1679 CB THR A 426 15.378 62.576 −2.410 1.00 32.58 A C ATOM 1680 OG1 THR A 426 15.125 62.807 −3.800 1.00 32.27 A O ATOM 1681 CG2 THR A 426 16.720 63.160 −2.040 1.00 31.56 A C ATOM 1682 C THR A 426 16.311 60.354 −3.036 1.00 33.13 A C ATOM 1683 O THR A 426 17.432 60.082 −2.632 1.00 31.17 A O ATOM 1684 N GLU A 427 15.876 60.044 −4.251 1.00 35.91 A N ATOM 1685 CA GLU A 427 16.755 59.478 −5.270 1.00 37.00 A C ATOM 1686 CB GLU A 427 16.119 58.245 −5.909 1.00 43.83 A C ATOM 1687 CG GLU A 427 15.904 57.126 −4.906 1.00 45.05 A C ATOM 1688 CD GLU A 427 15.774 55.779 −5.551 1.00 49.23 A C ATOM 1689 OE1 GLU A 427 14.854 55.597 −6.375 1.00 54.33 A O ATOM 1690 OE2 GLU A 427 16.593 54.900 −5.213 1.00 56.10 A O ATOM 1691 C GLU A 427 17.104 60.515 −6.337 1.00 37.10 A C ATOM 1692 O GLU A 427 17.824 60.227 −7.285 1.00 39.37 A O ATOM 1693 N GLY A 428 16.583 61.723 −6.177 1.00 33.88 A N ATOM 1694 CA GLY A 428 16.926 62.814 −7.060 1.00 32.25 A C ATOM 1695 C GLY A 428 18.179 63.533 −6.592 1.00 29.40 A C ATOM 1696 O GLY A 428 18.656 63.315 −5.479 1.00 33.20 A O ATOM 1697 N PRO A 429 18.739 64.389 −7.459 1.00 29.47 A N ATOM 1698 CD PRO A 429 18.330 64.539 −8.861 1.00 23.59 A C ATOM 1699 CA PRO A 429 19.892 65.232 −7.115 1.00 30.51 A C ATOM 1700 CB PRO A 429 19.923 66.260 −8.247 1.00 26.07 A C ATOM 1701 CG PRO A 429 19.297 65.582 −9.387 1.00 29.55 A C ATOM 1702 C PRO A 429 19.654 65.940 −5.774 1.00 31.41 A C ATOM 1703 O PRO A 429 18.658 66.646 −5.627 1.00 34.49 A O ATOM 1704 N PRO A 430 20.544 65.726 −4.806 1.00 25.43 A N ATOM 1705 CD PRO A 430 21.560 64.664 −4.902 1.00 28.97 A C ATOM 1706 CA PRO A 430 20.481 66.280 −3.457 1.00 27.18 A C ATOM 1707 CB PRO A 430 21.737 65.714 −2.722 1.00 29.51 A C ATOM 1708 CG PRO A 430 21.931 64.412 −3.480 1.00 26.73 A C ATOM 1709 C PRO A 430 20.498 67.796 −3.371 1.00 34.62 A C ATOM 1710 O PRO A 430 19.934 68.319 −2.408 1.00 27.76 A O ATOM 1711 N LEU A 431 21.109 68.509 −4.312 1.00 26.02 A N ATOM 1712 CA LEU A 431 21.226 69.958 −4.112 1.00 28.74 A C ATOM 1713 CB LEU A 431 22.519 70.527 −4.708 1.00 27.49 A C ATOM 1714 CG LEU A 431 23.836 70.202 −4.002 1.00 32.47 A C ATOM 1715 CD1 LEU A 431 25.025 70.610 −4.884 1.00 29.48 A C ATOM 1716 CD2 LEU A 431 23.902 70.900 −2.661 1.00 28.82 A C ATOM 1717 C LEU A 431 20.066 70.691 −4.712 1.00 21.45 A C ATOM 1718 O LEU A 431 19.533 70.264 −5.720 1.00 22.73 A O ATOM 1719 N HIS A 432 19.701 71.819 −4.103 1.00 26.85 A N ATOM 1720 CA HIS A 432 18.648 72.687 −4.646 1.00 27.16 A C ATOM 1721 CB HIS A 432 17.381 72.623 −3.801 1.00 29.72 A C ATOM 1722 CG HIS A 432 16.655 71.326 −3.909 1.00 28.53 A C ATOM 1723 CD2 HIS A 432 15.508 70.998 −4.546 1.00 26.74 A C ATOM 1724 ND1 HIS A 432 17.115 70.167 −3.317 1.00 28.99 A N ATOM 1725 CE1 HIS A 432 16.276 69.180 −3.580 1.00 24.72 A C ATOM 1726 NE2 HIS A 432 15.302 69.655 −4.336 1.00 24.94 A N ATOM 1727 C HIS A 432 19.086 74.122 −4.668 1.00 21.22 A C ATOM 1728 O HIS A 432 20.037 74.492 −4.004 1.00 27.85 A O ATOM 1729 N LYS A 433 18.358 74.933 −5.417 1.00 23.69 A N ATOM 1730 CA LYS A 433 18.703 76.332 −5.574 1.00 27.57 A C ATOM 1731 CB LYS A 433 17.525 77.102 −6.157 1.00 23.89 A C ATOM 1732 CG LYS A 433 17.109 76.590 −7.514 1.00 24.59 A C ATOM 1733 CD LYS A 433 15.835 77.303 −8.007 1.00 33.37 A C ATOM 1734 CE LYS A 433 15.445 76.925 −9.415 1.00 32.27 A C ATOM 1735 NZ LYS A 433 16.227 77.637 −10.467 1.00 31.36 A N ATOM 1736 C LYS A 433 19.141 76.925 −4.259 1.00 29.25 A C ATOM 1737 O LYS A 433 20.163 77.606 −4.178 1.00 27.37 A O ATOM 1738 N ASP A 434 18.382 76.662 −3.207 1.00 26.30 A N ATOM 1739 CA ASP A 434 18.692 77.297 −1.938 1.00 20.16 A C ATOM 1740 CB ASP A 434 17.624 76.987 −0.894 1.00 26.67 A C ATOM 1741 CG ASP A 434 17.737 77.888 0.297 1.00 21.35 A C ATOM 1742 OD1 ASP A 434 17.451 79.080 0.140 1.00 27.44 A O ATOM 1743 OD2 ASP A 434 18.156 77.418 1.365 1.00 26.80 A O ATOM 1744 C ASP A 434 20.060 76.894 −1.386 1.00 22.73 A C ATOM 1745 O ASP A 434 20.696 77.660 −0.650 1.00 22.33 A O ATOM 1746 N ASP A 435 20.468 75.667 −1.674 1.00 20.85 A N ATOM 1747 CA ASP A 435 21.771 75.174 −1.224 1.00 32.42 A C ATOM 1748 CB ASP A 435 21.843 73.630 −1.291 1.00 25.84 A C ATOM 1749 CG ASP A 435 20.665 72.940 −0.591 1.00 27.86 A C ATOM 1750 OD1 ASP A 435 20.477 73.148 0.626 1.00 27.89 A O ATOM 1751 OD2 ASP A 435 19.947 72.162 −1.261 1.00 30.11 A O ATOM 1752 C ASP A 435 22.902 75.826 −2.066 1.00 19.98 A C ATOM 1753 O ASP A 435 23.872 76.329 −1.517 1.00 28.25 A O ATOM 1754 N VAL A 436 22.743 75.830 −3.378 1.00 21.15 A N ATOM 1755 CA VAL A 436 23.727 76.448 −4.295 1.00 25.02 A C ATOM 1756 CB VAL A 436 23.354 76.186 −5.750 1.00 28.61 A C ATOM 1757 CG1 VAL A 436 24.301 76.936 −6.742 1.00 24.32 A C ATOM 1758 CG2 VAL A 436 23.350 74.692 −6.011 1.00 24.57 A C ATOM 1759 C VAL A 436 23.880 77.948 −4.059 1.00 30.75 A C ATOM 1760 O VAL A 436 24.996 78.457 −3.913 1.00 28.38 A O ATOM 1761 N ASN A 437 22.754 78.652 −3.970 1.00 27.73 A N ATOM 1762 CA ASN A 437 22.786 80.066 −3.658 1.00 21.15 A C ATOM 1763 CB ASN A 437 21.419 80.711 −3.841 1.00 33.13 A C ATOM 1764 CG ASN A 437 21.133 81.049 −5.281 1.00 38.24 A C ATOM 1765 OD1 ASN A 437 22.011 80.948 −6.142 1.00 39.84 A O ATOM 1766 ND2 ASN A 437 19.905 81.475 −5.559 1.00 34.85 A N ATOM 1767 C ASN A 437 23.370 80.360 −2.299 1.00 25.95 A C ATOM 1768 O ASN A 437 23.998 81.392 −2.111 1.00 31.39 A O ATOM 1769 N GLY A 438 23.218 79.449 −1.347 1.00 24.54 A N ATOM 1770 CA GLY A 438 23.779 79.686 −0.028 1.00 23.95 A C ATOM 1771 C GLY A 438 25.306 79.614 −0.064 1.00 32.24 A C ATOM 1772 O GLY A 438 26.022 80.422 0.529 1.00 33.98 A O ATOM 1773 N ILE A 439 25.807 78.609 −0.761 1.00 29.61 A N ATOM 1774 CA ILE A 439 27.244 78.372 −0.845 1.00 33.48 A C ATOM 1775 CB ILE A 439 27.523 76.938 −1.382 1.00 28.67 A C ATOM 1776 CG2 ILE A 439 27.394 76.895 −2.888 1.00 32.67 A C ATOM 1777 CG1 ILE A 439 28.860 76.398 −0.864 1.00 30.72 A C ATOM 1778 CD1 ILE A 439 28.959 76.339 0.649 1.00 27.98 A C ATOM 1779 C ILE A 439 27.899 79.482 −1.694 1.00 29.89 A C ATOM 1780 O ILE A 439 28.927 80.012 −1.321 1.00 36.80 A O ATOM 1781 N ARG A 440 27.270 79.873 −2.795 1.00 29.08 A N ATOM 1782 CA ARG A 440 27.752 81.020 −3.553 1.00 33.52 A C ATOM 1783 CB ARG A 440 26.868 81.329 −4.766 1.00 30.06 A C ATOM 1784 CG ARG A 440 26.976 80.276 −5.844 1.00 35.84 A C ATOM 1785 CD ARG A 440 26.382 80.721 −7.163 1.00 33.90 A C ATOM 1786 NE ARG A 440 27.097 81.869 −7.712 1.00 37.11 A N ATOM 1787 CZ ARG A 440 26.905 82.328 −8.945 1.00 38.23 A C ATOM 1788 NH1 ARG A 440 26.016 81.754 −9.736 1.00 42.76 A N ATOM 1789 NH2 ARG A 440 27.597 83.357 −9.391 1.00 43.96 A N ATOM 1790 C ARG A 440 27.889 82.229 −2.652 1.00 41.32 A C ATOM 1791 O ARG A 440 28.950 82.849 −2.620 1.00 44.45 A O ATOM 1792 N HIS A 441 26.837 82.546 −1.895 1.00 40.88 A N ATOM 1793 CA HIS A 441 26.853 83.709 −0.994 1.00 38.08 A C ATOM 1794 CB HIS A 441 25.477 83.968 −0.372 1.00 36.49 A C ATOM 1795 CG HIS A 441 24.410 84.259 −1.377 1.00 36.13 A C ATOM 1796 CD2 HIS A 441 23.066 84.100 −1.322 1.00 36.79 A C ATOM 1797 ND1 HIS A 441 24.686 84.787 −2.619 1.00 39.18 A N ATOM 1798 CE1 HIS A 441 23.557 84.928 −3.295 1.00 41.38 A C ATOM 1799 NE2 HIS A 441 22.560 84.527 −2.527 1.00 42.62 A N ATOM 1800 C HIS A 441 27.873 83.605 0.119 1.00 38.30 A C ATOM 1801 O HIS A 441 27.881 84.437 1.019 1.00 39.90 A O ATOM 1802 N LEU A 442 28.715 82.580 0.079 1.00 37.40 A N ATOM 1803 CA LEU A 442 29.740 82.414 1.104 1.00 36.58 A C ATOM 1804 CB LEU A 442 29.554 81.082 1.836 1.00 34.94 A C ATOM 1805 CG LEU A 442 29.676 81.101 3.366 1.00 38.08 A C ATOM 1806 CD1 LEU A 442 29.424 79.718 4.011 1.00 34.32 A C ATOM 1807 CD2 LEU A 442 31.024 81.656 3.791 1.00 44.31 A C ATOM 1808 C LEU A 442 31.147 82.470 0.506 1.00 40.31 A C ATOM 1809 O LEU A 442 32.047 83.085 1.073 1.00 42.88 A O ATOM 1810 N TYR A 443 31.322 81.823 −0.643 1.00 35.05 A N ATOM 1811 CA TYR A 443 32.639 81.653 −1.274 1.00 40.92 A C ATOM 1812 CB TYR A 443 32.996 80.154 −1.373 1.00 30.92 A C ATOM 1813 CG TYR A 443 33.294 79.534 −0.027 1.00 35.32 A C ATOM 1814 CD1 TYR A 443 32.384 78.681 0.587 1.00 32.49 A C ATOM 1815 CE1 TYR A 443 32.655 78.105 1.823 1.00 26.61 A C ATOM 1816 CD2 TYR A 443 34.489 79.811 0.647 1.00 34.15 A C ATOM 1817 CE2 TYR A 443 34.755 79.253 1.884 1.00 36.38 A C ATOM 1818 CZ TYR A 443 33.821 78.403 2.474 1.00 31.16 A C ATOM 1819 OH TYR A 443 34.077 77.846 3.706 1.00 30.00 A O ATOM 1820 C TYR A 443 32.747 82.320 −2.651 1.00 41.25 A C ATOM 1821 O TYR A 443 31.742 82.533 −3.340 1.00 45.93 A O ATOM 1822 ZN ZN A 500 22.102 70.114 9.863 1.00 30.01 A Zn ATOM 1823 ZN ZN A 501 30.065 64.798 18.002 1.00 39.36 A Zn ATOM 1824 CA CA A 502 20.282 58.923 16.938 1.00 35.28 A Ca ATOM 1825 CA CA A 504 38.880 70.297 12.131 1.00 51.74 A Ca ATOM 1826 CA CA A 505 41.748 78.476 7.140 1.00 52.17 A Ca TER 1827 CA A 505 ATOM 1828 CB ASP B 41 5.022 13.505 39.326 1.00 65.74 B C ATOM 1829 CG ASP B 41 4.163 13.796 38.118 1.00 65.95 B C ATOM 1830 OD1 ASP B 41 4.201 13.001 37.155 1.00 59.17 B O ATOM 1831 OD2 ASP B 41 3.464 14.831 38.126 1.00 68.82 B O ATOM 1832 C ASP B 41 5.571 15.898 39.892 1.00 71.04 B C ATOM 1833 O ASP B 41 5.670 16.867 39.134 1.00 65.93 B O ATOM 1834 N ASP B 41 7.108 14.067 40.496 1.00 67.20 B N ATOM 1835 CA ASP B 41 6.142 14.531 39.506 1.00 70.21 B C ATOM 1836 N ARG B 42 4.958 15.960 41.071 1.00 75.25 B N ATOM 1837 CA ARG B 42 4.633 17.236 41.701 1.00 74.37 B C ATOM 1838 CB ARG B 42 3.765 17.009 42.944 1.00 74.29 B C ATOM 1839 CG ARG B 42 3.788 18.156 43.960 1.00 75.37 B C ATOM 1840 CD ARG B 42 2.682 19.175 43.702 1.00 76.78 B C ATOM 1841 NE ARG B 42 2.713 20.283 44.659 1.00 78.96 B N ATOM 1842 CZ ARG B 42 1.761 21.208 44.768 1.00 80.51 B C ATOM 1843 NH1 ARG B 42 0.690 21.153 43.982 1.00 80.92 B N ATOM 1844 NH2 ARG B 42 1.874 22.182 45.665 1.00 76.45 B N ATOM 1845 C ARG B 42 5.946 17.924 42.096 1.00 74.15 B C ATOM 1846 O ARG B 42 6.054 19.160 42.079 1.00 70.08 B O ATOM 1847 N GLN B 43 6.937 17.098 42.448 1.00 72.25 B N ATOM 1848 CA GLN B 43 8.264 17.567 42.828 1.00 68.50 B C ATOM 1849 CB GLN B 43 9.092 16.409 43.394 1.00 67.70 B C ATOM 1850 CG GLN B 43 8.289 15.342 44.158 1.00 71.84 B C ATOM 1851 CD GLN B 43 7.766 14.228 43.258 1.00 71.97 B C ATOM 1852 OE1 GLN B 43 8.534 13.566 42.553 1.00 72.75 B O ATOM 1853 NE2 GLN B 43 6.456 14.012 43.285 1.00 71.19 B N ATOM 1854 C GLN B 43 8.935 18.101 41.576 1.00 67.06 B C ATOM 1855 O GLN B 43 9.571 19.159 41.573 1.00 61.43 B O ATOM 1856 N LEU B 44 8.777 17.344 40.505 1.00 63.74 B N ATOM 1857 CA LEU B 44 9.273 17.753 39.219 1.00 62.74 B C ATOM 1858 CB LEU B 44 8.858 16.728 38.172 1.00 64.04 B C ATOM 1859 CG LEU B 44 9.538 16.825 36.811 1.00 67.58 B C ATOM 1860 CD1 LEU B 44 9.472 15.488 36.057 1.00 67.66 B C ATOM 1861 CD2 LEU B 44 8.902 17.947 36.013 1.00 63.50 B C ATOM 1862 C LEU B 44 8.713 19.127 38.883 1.00 63.84 B C ATOM 1863 O LEU B 44 9.465 20.070 38.661 1.00 61.49 B O ATOM 1864 N ALA B 45 7.393 19.247 38.855 1.00 61.91 B N ATOM 1865 CA ALA B 45 6.775 20.505 38.471 1.00 58.80 B C ATOM 1866 CB ALA B 45 5.274 20.410 38.579 1.00 61.07 B C ATOM 1867 C ALA B 45 7.300 21.665 39.310 1.00 60.91 B C ATOM 1868 O ALA B 45 7.666 22.711 38.772 1.00 57.10 B O ATOM 1869 N GLU B 46 7.341 21.475 40.627 1.00 63.09 B N ATOM 1870 CA GLU B 46 7.750 22.538 41.542 1.00 59.47 B C ATOM 1871 CB GLU B 46 7.679 22.058 42.994 1.00 63.75 B C ATOM 1872 CG GLU B 46 6.283 22.073 43.593 1.00 70.09 B C ATOM 1873 CD GLU B 46 6.276 21.760 45.081 1.00 72.04 B C ATOM 1874 OE1 GLU B 46 7.247 21.145 45.577 1.00 73.57 B O ATOM 1875 OE2 GLU B 46 5.294 22.127 45.756 1.00 72.41 B O ATOM 1876 C GLU B 46 9.155 23.025 41.254 1.00 55.36 B C ATOM 1877 O GLU B 46 9.408 24.226 41.209 1.00 55.17 B O ATOM 1878 N GLU B 47 10.068 22.077 41.085 1.00 57.58 B N ATOM 1879 CA GLU B 47 11.481 22.367 40.862 1.00 59.64 B C ATOM 1880 CB GLU B 47 12.249 21.047 40.771 1.00 61.53 B C ATOM 1881 CG GLU B 47 13.714 21.134 41.132 1.00 67.83 B C ATOM 1882 CD GLU B 47 14.490 22.033 40.192 1.00 70.62 B C ATOM 1883 OE1 GLU B 47 14.383 21.838 38.955 1.00 70.87 B O ATOM 1884 OE2 GLU B 47 15.209 22.934 40.694 1.00 71.51 B O ATOM 1885 C GLU B 47 11.679 23.186 39.584 1.00 54.79 B C ATOM 1886 O GLU B 47 12.296 24.250 39.604 1.00 53.75 B O ATOM 1887 N TYR B 48 11.138 22.676 38.480 1.00 53.13 B N ATOM 1888 CA TYR B 48 11.179 23.342 37.177 1.00 51.61 B C ATOM 1889 CB TYR B 48 10.327 22.550 36.178 1.00 44.62 B C ATOM 1890 CG TYR B 48 10.500 22.920 34.719 1.00 48.44 B C ATOM 1891 CD1 TYR B 48 10.205 24.195 34.263 1.00 45.42 B C ATOM 1892 CE1 TYR B 48 10.350 24.536 32.916 1.00 43.59 B C ATOM 1893 CD2 TYR B 48 10.928 21.976 33.786 1.00 49.68 B C ATOM 1894 CE2 TYR B 48 11.072 22.304 32.434 1.00 42.42 B C ATOM 1895 CZ TYR B 48 10.790 23.589 32.012 1.00 40.58 B C ATOM 1896 OH TYR B 48 10.912 23.927 30.688 1.00 34.82 B O ATOM 1897 C TYR B 48 10.696 24.793 37.272 1.00 52.17 B C ATOM 1898 O TYR B 48 11.434 25.730 36.958 1.00 49.81 B O ATOM 1899 N LEU B 49 9.459 24.978 37.720 1.00 49.77 B N ATOM 1900 CA LEU B 49 8.882 26.310 37.832 1.00 46.45 B C ATOM 1901 CB LEU B 49 7.519 26.256 38.519 1.00 51.02 B C ATOM 1902 CG LEU B 49 6.387 25.614 37.731 1.00 53.12 B C ATOM 1903 CD1 LEU B 49 5.252 25.193 38.662 1.00 60.04 B C ATOM 1904 CD2 LEU B 49 5.901 26.582 36.681 1.00 51.92 B C ATOM 1905 C LEU B 49 9.780 27.225 38.624 1.00 46.54 B C ATOM 1906 O LEU B 49 9.854 28.420 38.350 1.00 49.92 B O ATOM 1907 N TYR B 50 10.445 26.685 39.636 1.00 42.96 B N ATOM 1908 CA TYR B 50 11.263 27.548 40.472 1.00 45.93 B C ATOM 1909 CB TYR B 50 11.610 26.902 41.815 1.00 50.35 B C ATOM 1910 CG TYR B 50 12.649 27.709 42.563 1.00 52.07 B C ATOM 1911 CD1 TYR B 50 12.288 28.832 43.292 1.00 55.31 B C ATOM 1912 CE1 TYR B 50 13.240 29.596 43.962 1.00 56.70 B C ATOM 1913 CD2 TYR B 50 13.998 27.374 42.504 1.00 54.61 B C ATOM 1914 CE2 TYR B 50 14.961 28.130 43.167 1.00 55.56 B C ATOM 1915 CZ TYR B 50 14.575 29.242 43.899 1.00 59.82 B C ATOM 1916 OH TYR B 50 15.524 30.003 44.565 1.00 65.40 B O ATOM 1917 C TYR B 50 12.538 27.912 39.736 1.00 51.95 B C ATOM 1918 O TYR B 50 12.943 29.081 39.713 1.00 51.35 B O ATOM 1919 N ARG B 51 13.160 26.897 39.136 1.00 54.54 B N ATOM 1920 CA ARG B 51 14.479 27.029 38.509 1.00 52.84 B C ATOM 1921 CB ARG B 51 14.880 25.711 37.845 1.00 49.30 B C ATOM 1922 CG ARG B 51 16.279 25.694 37.246 1.00 47.56 B C ATOM 1923 CD ARG B 51 16.503 24.426 36.436 1.00 45.80 B C ATOM 1924 NE ARG B 51 16.868 23.265 37.250 1.00 46.98 B N ATOM 1925 CZ ARG B 51 18.080 23.053 37.759 1.00 50.08 B C ATOM 1926 NH1 ARG B 51 19.057 23.937 37.567 1.00 41.56 B N ATOM 1927 NH2 ARG B 51 18.314 21.959 38.480 1.00 52.18 B N ATOM 1928 C ARG B 51 14.488 28.130 37.470 1.00 44.39 B C ATOM 1929 O ARG B 51 15.373 28.992 37.452 1.00 40.15 B O ATOM 1930 N TYR B 52 13.480 28.105 36.616 1.00 43.93 B N ATOM 1931 CA TYR B 52 13.486 28.956 35.448 1.00 40.69 B C ATOM 1932 CB TYR B 52 12.863 28.216 34.270 1.00 43.23 B C ATOM 1933 CG TYR B 52 13.625 26.934 33.970 1.00 44.97 B C ATOM 1934 CD1 TYR B 52 13.067 25.690 34.227 1.00 41.85 B C ATOM 1935 CE1 TYR B 52 13.770 24.517 33.967 1.00 44.90 B C ATOM 1936 CD2 TYR B 52 14.921 26.976 33.465 1.00 39.45 B C ATOM 1937 CE2 TYR B 52 15.638 25.809 33.215 1.00 38.75 B C ATOM 1938 CZ TYR B 52 15.055 24.582 33.457 1.00 44.77 B C ATOM 1939 OH TYR B 52 15.756 23.417 33.201 1.00 47.32 B O ATOM 1940 C TYR B 52 12.871 30.317 35.680 1.00 44.92 B C ATOM 1941 O TYR B 52 12.693 31.070 34.730 1.00 38.50 B O ATOM 1942 N GLY B 53 12.547 30.617 36.946 1.00 52.40 B N ATOM 1943 CA GLY B 53 12.119 31.953 37.375 1.00 52.23 B C ATOM 1944 C GLY B 53 10.620 32.214 37.516 1.00 53.39 B C ATOM 1945 O GLY B 53 10.201 33.341 37.800 1.00 51.02 B O ATOM 1946 N TYR B 54 9.818 31.170 37.329 1.00 46.47 B N ATOM 1947 CA TYR B 54 8.361 31.285 37.312 1.00 53.09 B C ATOM 1948 CB TYR B 54 7.752 29.995 36.748 1.00 48.72 B C ATOM 1949 CG TYR B 54 8.006 29.871 35.269 1.00 49.41 B C ATOM 1950 CD1 TYR B 54 8.884 28.910 34.753 1.00 52.68 B C ATOM 1951 CE1 TYR B 54 9.131 28.830 33.389 1.00 42.25 B C ATOM 1952 CD2 TYR B 54 7.406 30.751 34.386 1.00 47.29 B C ATOM 1953 CE2 TYR B 54 7.643 30.681 33.043 1.00 48.96 B C ATOM 1954 CZ TYR B 54 8.499 29.725 32.547 1.00 46.11 B C ATOM 1955 OH TYR B 54 8.698 29.695 31.195 1.00 44.01 B O ATOM 1956 C TYR B 54 7.735 31.652 38.670 1.00 58.21 B C ATOM 1957 O TYR B 54 7.173 32.743 38.850 1.00 51.66 B O ATOM 1958 N THR B 55 7.826 30.736 39.620 1.00 52.97 B N ATOM 1959 CA THR B 55 7.336 31.011 40.950 1.00 54.51 B C ATOM 1960 CB THR B 55 7.827 29.949 41.923 1.00 53.92 B C ATOM 1961 OG1 THR B 55 9.163 30.268 42.319 1.00 57.98 B O ATOM 1962 CG2 THR B 55 7.798 28.557 41.265 1.00 43.39 B C ATOM 1963 C THR B 55 7.804 32.403 41.409 1.00 61.71 B C ATOM 1964 O THR B 55 7.003 33.235 41.845 1.00 65.02 B O ATOM 1965 N ARG B 56 9.098 32.662 41.284 1.00 57.06 B N ATOM 1966 CA ARG B 56 9.700 33.907 41.764 1.00 63.01 B C ATOM 1967 CB ARG B 56 11.191 33.901 41.422 1.00 66.89 B C ATOM 1968 CG ARG B 56 11.964 35.173 41.742 1.00 72.53 B C ATOM 1969 CD ARG B 56 13.434 34.976 41.357 1.00 77.67 B C ATOM 1970 NE ARG B 56 14.348 35.771 42.171 1.00 81.82 B N ATOM 1971 CZ ARG B 56 15.591 35.402 42.465 1.00 79.88 B C ATOM 1972 NH1 ARG B 56 16.066 34.244 42.016 1.00 73.79 B N ATOM 1973 NH2 ARG B 56 16.356 36.187 43.216 1.00 78.98 B N ATOM 1974 C ARG B 56 9.049 35.165 41.191 1.00 63.81 B C ATOM 1975 O ARG B 56 9.086 36.231 41.797 1.00 64.42 B O ATOM 1976 N VAL B 57 8.470 35.046 40.008 1.00 63.79 B N ATOM 1977 CA VAL B 57 7.896 36.200 39.352 1.00 61.30 B C ATOM 1978 CB VAL B 57 8.110 36.147 37.840 1.00 59.39 B C ATOM 1979 CG1 VAL B 57 7.166 37.099 37.134 1.00 64.11 B C ATOM 1980 CG2 VAL B 57 9.564 36.482 37.514 1.00 58.75 B C ATOM 1981 C VAL B 57 6.424 36.235 39.668 1.00 66.96 B C ATOM 1982 O VAL B 57 5.817 37.306 39.733 1.00 71.03 B O ATOM 1983 N ALA B 58 5.852 35.054 39.876 1.00 64.11 B N ATOM 1984 CA ALA B 58 4.482 34.954 40.352 1.00 61.65 B C ATOM 1985 CB ALA B 58 4.073 33.503 40.486 1.00 65.52 B C ATOM 1986 C ALA B 58 4.388 35.677 41.696 1.00 67.74 B C ATOM 1987 O ALA B 58 3.712 36.699 41.812 1.00 67.71 B O ATOM 1988 N GLU B 59 5.081 35.149 42.702 1.00 67.67 N ATOM 1989 CA GLU B 59 5.206 35.834 43.982 1.00 65.60 C ATOM 1990 C GLU B 59 5.372 37.325 43.727 1.00 67.86 C ATOM 1991 CB GLU B 59 6.413 35.307 44.765 1.00 58.06 C ATOM 1992 CG GLU B 59 6.392 33.812 45.045 1.00 59.37 C ATOM 1993 CD GLU B 59 7.649 33.339 45.772 1.00 60.63 C ATOM 1994 OE1 GLU B 59 8.658 34.084 45.773 1.00 63.25 O ATOM 1995 OE2 GLU B 59 7.634 32.227 46.347 1.00 56.75 O ATOM 1996 O GLU B 59 4.413 38.086 43.784 1.00 73.68 O ATOM 1997 N MET B 60 6.600 37.730 43.427 1.00 67.55 N ATOM 1998 CA MET B 60 6.918 39.118 43.114 1.00 69.87 C ATOM 1999 C MET B 60 5.934 39.739 42.141 1.00 76.80 C ATOM 2000 CB MET B 60 8.324 39.204 42.515 1.00 79.28 C ATOM 2001 CG MET B 60 8.656 40.537 41.849 1.00 83.24 C ATOM 2002 SD MET B 60 10.117 40.403 40.796 1.00 89.28 S ATOM 2003 CE MET B 60 10.466 42.135 40.471 1.00 84.15 C ATOM 2004 O MET B 60 6.051 39.531 40.931 1.00 76.81 O ATOM 2005 N ARG B 61 4.971 40.483 42.689 1.00 80.76 N ATOM 2006 CA ARG B 61 4.034 41.338 41.941 1.00 80.02 C ATOM 2007 C ARG B 61 2.561 40.920 42.057 1.00 82.28 C ATOM 2008 CB ARG B 61 4.445 41.534 40.462 1.00 85.16 C ATOM 2009 CG ARG B 61 3.930 40.470 39.477 1.00 80.22 C ATOM 2010 CD ARG B 61 4.384 40.760 38.050 1.00 78.02 C ATOM 2011 NE ARG B 61 3.909 39.753 37.099 1.00 80.81 N ATOM 2012 CZ ARG B 61 3.946 39.897 35.775 1.00 78.21 C ATOM 2013 NH1 ARG B 61 4.436 41.010 35.241 1.00 80.01 N ATOM 2014 NH2 ARG B 61 3.491 38.930 34.985 1.00 66.52 N ATOM 2015 O ARG B 61 1.690 41.768 42.261 1.00 84.66 O ATOM 2016 N GLY B 62 2.283 39.625 41.936 1.00 79.93 N ATOM 2017 CA GLY B 62 0.906 39.176 41.832 1.00 83.57 C ATOM 2018 C GLY B 62 0.499 38.021 42.726 1.00 88.38 C ATOM 2019 O GLY B 62 −0.004 37.003 42.237 1.00 91.14 O ATOM 2020 O ALA B 63 1.504 35.177 45.204 1.00 83.74 O ATOM 2021 N ALA B 63 0.710 38.179 44.032 1.00 87.30 N ATOM 2022 CA ALA B 63 0.235 37.217 45.036 1.00 84.21 C ATOM 2023 C ALA B 63 0.522 35.744 44.716 1.00 82.02 C ATOM 2024 CB ALA B 63 −1.256 37.424 45.314 1.00 81.80 C ATOM 2025 O ALA B 64 0.555 32.582 45.554 1.00 82.36 O ATOM 2026 N ALA B 64 −0.349 35.131 43.916 1.00 80.13 N ATOM 2027 CA ALA B 64 −0.246 33.712 43.575 1.00 79.65 C ATOM 2028 C ALA B 64 −0.398 32.794 44.795 1.00 80.69 C ATOM 2029 CB ALA B 64 1.060 33.432 42.845 1.00 79.23 C ATOM 2030 O ALA B 65 −0.096 29.771 46.514 1.00 75.70 O ATOM 2031 N ALA B 65 −1.597 32.244 44.975 1.00 77.24 N ATOM 2032 CA ALA B 65 −1.867 31.342 46.091 1.00 78.75 C ATOM 2033 C ALA B 65 −1.150 30.003 45.914 1.00 76.00 C ATOM 2034 CB ALA B 65 −3.373 31.134 46.259 1.00 78.89 C ATOM 2035 N SER B 66 −1.722 29.129 45.091 1.00 74.14 N ATOM 2036 CA SER B 66 −1.083 27.859 44.752 1.00 76.20 C ATOM 2037 C SER B 66 −0.200 28.045 43.526 1.00 76.11 C ATOM 2038 CB SER B 66 −2.126 26.790 44.437 1.00 74.06 C ATOM 2039 OG SER B 66 −2.584 26.917 43.099 1.00 72.23 O ATOM 2040 O SER B 66 −0.069 29.156 43.011 1.00 75.48 O ATOM 2041 N LEU B 67 0.396 26.958 43.049 1.00 73.68 N ATOM 2042 CA LEU B 67 1.195 27.032 41.831 1.00 73.20 C ATOM 2043 C LEU B 67 0.316 26.958 40.571 1.00 71.75 C ATOM 2044 CB LEU B 67 2.321 25.984 41.827 1.00 70.14 C ATOM 2045 CG LEU B 67 2.049 24.531 42.229 1.00 72.69 C ATOM 2046 CD1 LEU B 67 1.458 23.735 41.074 1.00 66.99 C ATOM 2047 CD2 LEU B 67 3.336 23.886 42.713 1.00 69.48 C ATOM 2048 O LEU B 67 0.685 26.334 39.576 1.00 69.22 O ATOM 2049 N GLY B 68 −0.842 27.616 40.629 1.00 71.30 B N ATOM 2050 CA GLY B 68 −1.745 27.727 39.493 1.00 63.45 B C ATOM 2051 C GLY B 68 −1.452 28.943 38.628 1.00 66.35 B C ATOM 2052 O GLY B 68 −1.557 28.865 37.402 1.00 64.85 B O ATOM 2053 N PRO B 69 −1.115 30.084 39.261 1.00 68.38 B N ATOM 2054 CD PRO B 69 −1.466 30.386 40.660 1.00 70.73 B C ATOM 2055 CA PRO B 69 −0.577 31.268 38.577 1.00 69.12 B C ATOM 2056 CB PRO B 69 −0.463 32.302 39.708 1.00 71.10 B C ATOM 2057 CG PRO B 69 −1.480 31.889 40.692 1.00 71.67 B C ATOM 2058 C PRO B 69 0.804 31.023 37.942 1.00 62.19 B C ATOM 2059 O PRO B 69 0.985 31.287 36.753 1.00 56.18 B O ATOM 2060 N ALA B 70 1.758 30.529 38.726 1.00 61.70 B N ATOM 2061 CA ALA B 70 3.081 30.203 38.202 1.00 57.78 B C ATOM 2062 CB ALA B 70 3.980 29.643 39.296 1.00 55.65 B C ATOM 2063 C ALA B 70 3.022 29.245 37.014 1.00 57.58 B C ATOM 2064 O ALA B 70 3.912 29.260 36.167 1.00 58.50 B O ATOM 2065 N LEU B 71 1.979 28.423 36.937 1.00 58.37 B N ATOM 2066 CA LEU B 71 1.845 27.484 35.825 1.00 54.20 B C ATOM 2067 CB LEU B 71 0.981 26.293 36.217 1.00 57.73 B C ATOM 2068 CG LEU B 71 1.740 25.038 36.643 1.00 61.95 B C ATOM 2069 CD1 LEU B 71 0.804 23.995 37.236 1.00 63.87 B C ATOM 2070 CD2 LEU B 71 2.474 24.462 35.456 1.00 60.55 B C ATOM 2071 C LEU B 71 1.301 28.114 34.547 1.00 57.56 B C ATOM 2072 O LEU B 71 1.513 27.594 33.449 1.00 54.38 B O ATOM 2073 N LEU B 72 0.585 29.225 34.679 1.00 59.26 B N ATOM 2074 CA LEU B 72 0.057 29.892 33.494 1.00 58.25 B C ATOM 2075 CB LEU B 72 −1.160 30.759 33.833 1.00 52.93 B C ATOM 2076 CG LEU B 72 −2.275 30.715 32.782 1.00 58.95 B C ATOM 2077 CD1 LEU B 72 −3.393 31.721 33.058 1.00 59.88 B C ATOM 2078 CD2 LEU B 72 −2.843 29.307 32.668 1.00 59.13 B C ATOM 2079 C LEU B 72 1.150 30.731 32.842 1.00 49.05 B C ATOM 2080 O LEU B 72 1.232 30.816 31.624 1.00 51.22 B O ATOM 2081 N LEU B 73 1.974 31.364 33.666 1.00 52.29 B N ATOM 2082 CA LEU B 73 3.126 32.094 33.169 1.00 50.42 B C ATOM 2083 CB LEU B 73 3.957 32.621 34.330 1.00 43.90 B C ATOM 2084 CG LEU B 73 3.362 33.801 35.082 1.00 47.42 B C ATOM 2085 CD1 LEU B 73 4.385 34.352 36.050 1.00 47.82 B C ATOM 2086 CD2 LEU B 73 2.892 34.867 34.104 1.00 45.81 B C ATOM 2087 C LEU B 73 3.975 31.151 32.324 1.00 48.66 B C ATOM 2088 O LEU B 73 4.338 31.459 31.195 1.00 39.99 B O ATOM 2089 N LEU B 74 4.274 29.988 32.889 1.00 46.40 B N ATOM 2090 CA LEU B 74 5.084 29.002 32.200 1.00 47.76 B C ATOM 2091 CB LEU B 74 5.289 27.770 33.072 1.00 46.03 B C ATOM 2092 CG LEU B 74 5.643 26.549 32.238 1.00 48.51 B C ATOM 2093 CD1 LEU B 74 6.809 25.776 32.853 1.00 50.36 B C ATOM 2094 CD2 LEU B 74 4.422 25.677 32.046 1.00 46.77 B C ATOM 2095 C LEU B 74 4.473 28.603 30.872 1.00 50.10 B C ATOM 2096 O LEU B 74 5.164 28.538 29.854 1.00 49.27 B O ATOM 2097 N GLN B 75 3.175 28.337 30.886 1.00 48.13 B N ATOM 2098 CA GLN B 75 2.471 27.924 29.687 1.00 46.79 B C ATOM 2099 CB GLN B 75 1.044 27.513 30.033 1.00 55.32 B C ATOM 2100 CG GLN B 75 0.961 26.281 30.922 1.00 55.15 B C ATOM 2101 CD GLN B 75 −0.454 26.005 31.381 1.00 59.47 B C ATOM 2102 OE1 GLN B 75 −1.109 26.868 31.983 1.00 54.32 B O ATOM 2103 NE2 GLN B 75 −0.935 24.801 31.099 1.00 59.22 B N ATOM 2104 C GLN B 75 2.451 29.056 28.679 1.00 45.24 B C ATOM 2105 O GLN B 75 2.353 28.823 27.475 1.00 44.89 B O ATOM 2106 N LYS B 76 2.526 30.285 29.169 1.00 43.52 B N ATOM 2107 CA LYS B 76 2.630 31.416 28.261 1.00 48.29 B C ATOM 2108 CB LYS B 76 2.364 32.740 28.976 1.00 52.99 B C ATOM 2109 CG LYS B 76 0.887 32.980 29.294 1.00 59.68 B C ATOM 2110 CD LYS B 76 0.614 34.454 29.615 1.00 69.17 B C ATOM 2111 CE LYS B 76 −0.829 34.682 30.086 1.00 67.84 B C ATOM 2112 NZ LYS B 76 −1.075 34.064 31.420 1.00 62.54 B N ATOM 2113 C LYS B 76 4.006 31.425 27.587 1.00 46.35 B C ATOM 2114 O LYS B 76 4.089 31.387 26.365 1.00 41.00 B O ATOM 2115 N GLN B 77 5.068 31.454 28.388 1.00 47.54 B N ATOM 2116 CA GLN B 77 6.447 31.453 27.867 1.00 50.61 B C ATOM 2117 CB GLN B 77 7.463 31.323 29.002 1.00 48.68 B C ATOM 2118 CG GLN B 77 7.977 32.651 29.524 1.00 55.06 B C ATOM 2119 CD GLN B 77 8.596 33.511 28.434 1.00 56.24 B C ATOM 2120 OE1 GLN B 77 8.521 34.741 28.478 1.00 59.18 B O ATOM 2121 NE2 GLN B 77 9.215 32.866 27.448 1.00 53.94 B N ATOM 2122 C GLN B 77 6.746 30.377 26.823 1.00 46.16 B C ATOM 2123 O GLN B 77 7.472 30.630 25.880 1.00 49.02 B O ATOM 2124 N LEU B 78 6.188 29.183 26.993 1.00 43.35 B N ATOM 2125 CA LEU B 78 6.489 28.067 26.106 1.00 43.42 B C ATOM 2126 CB LEU B 78 6.595 26.769 26.903 1.00 41.38 B C ATOM 2127 CG LEU B 78 7.361 26.948 28.208 1.00 39.55 B C ATOM 2128 CD1 LEU B 78 7.865 25.622 28.707 1.00 40.76 B C ATOM 2129 CD2 LEU B 78 8.508 27.929 28.019 1.00 42.89 B C ATOM 2130 C LEU B 78 5.436 27.917 25.030 1.00 42.27 B C ATOM 2131 O LEU B 78 5.441 26.948 24.270 1.00 38.83 B O ATOM 2132 N SER B 79 4.539 28.891 24.959 1.00 41.22 B N ATOM 2133 CA SER B 79 3.379 28.785 24.087 1.00 43.16 B C ATOM 2134 CB SER B 79 3.756 29.107 22.647 1.00 42.01 B C ATOM 2135 OG SER B 79 3.905 30.508 22.521 1.00 46.07 B O ATOM 2136 C SER B 79 2.725 27.414 24.210 1.00 38.43 B C ATOM 2137 O SER B 79 2.514 26.712 23.213 1.00 39.79 B O ATOM 2138 N LEU B 80 2.435 27.044 25.460 1.00 43.42 B N ATOM 2139 CA LEU B 80 1.599 25.882 25.806 1.00 50.55 B C ATOM 2140 CB LEU B 80 2.082 25.257 27.113 1.00 45.61 B C ATOM 2141 CG LEU B 80 3.505 24.727 27.060 1.00 43.90 B C ATOM 2142 CD1 LEU B 80 3.922 24.228 28.424 1.00 44.53 B C ATOM 2143 CD2 LEU B 80 3.613 23.627 26.000 1.00 48.00 B C ATOM 2144 C LEU B 80 0.142 26.301 25.989 1.00 45.27 B C ATOM 2145 O LEU B 80 −0.128 27.484 26.200 1.00 45.06 B O ATOM 2146 N PRO B 81 −0.798 25.336 25.913 1.00 48.19 B N ATOM 2147 CD PRO B 81 −0.655 23.918 25.539 1.00 53.09 B C ATOM 2148 CA PRO B 81 −2.180 25.655 26.285 1.00 57.06 B C ATOM 2149 CB PRO B 81 −2.870 24.285 26.296 1.00 56.36 B C ATOM 2150 CG PRO B 81 −2.083 23.460 25.359 1.00 53.06 B C ATOM 2151 C PRO B 81 −2.183 26.250 27.684 1.00 54.09 B C ATOM 2152 O PRO B 81 −1.569 25.671 28.595 1.00 53.23 B O ATOM 2153 N GLU B 82 −2.837 27.400 27.835 1.00 52.51 B N ATOM 2154 CA GLU B 82 −2.826 28.132 29.090 1.00 55.86 B C ATOM 2155 CB GLU B 82 −2.993 29.620 28.812 1.00 58.20 B C ATOM 2156 CG GLU B 82 −2.190 30.111 27.630 1.00 54.39 B C ATOM 2157 CD GLU B 82 −2.002 31.608 27.662 1.00 59.82 B C ATOM 2158 OE1 GLU B 82 −2.005 32.164 28.778 1.00 61.53 B O ATOM 2159 OE2 GLU B 82 −1.853 32.227 26.583 1.00 58.32 B O ATOM 2160 C GLU B 82 −3.926 27.630 30.026 1.00 58.62 B C ATOM 2161 O GLU B 82 −4.807 28.383 30.439 1.00 56.46 B O ATOM 2162 N THR B 83 −3.861 26.348 30.357 1.00 58.32 B N ATOM 2163 CA THR B 83 −4.911 25.711 31.133 1.00 57.05 B C ATOM 2164 CB THR B 83 −4.912 24.169 30.938 1.00 53.64 B C ATOM 2165 OG1 THR B 83 −3.769 23.590 31.571 1.00 57.63 B O ATOM 2166 CG2 THR B 83 −4.912 23.814 29.466 1.00 51.79 B C ATOM 2167 C THR B 83 −4.845 26.080 32.620 1.00 59.66 B C ATOM 2168 O THR B 83 −5.875 26.166 33.285 1.00 67.34 B O ATOM 2169 N GLY B 84 −3.644 26.326 33.131 1.00 56.50 B N ATOM 2170 CA GLY B 84 −3.456 26.611 34.545 1.00 56.74 B C ATOM 2171 C GLY B 84 −3.260 25.327 35.334 1.00 64.07 B C ATOM 2172 O GLY B 84 −2.985 25.345 36.540 1.00 60.41 B O ATOM 2173 N GLU B 85 −3.397 24.206 34.631 1.00 63.09 B N ATOM 2174 CA GLU B 85 −3.299 22.879 35.216 1.00 59.41 B C ATOM 2175 CB GLU B 85 −4.203 21.924 34.438 1.00 60.22 B C ATOM 2176 CG GLU B 85 −5.690 22.246 34.529 1.00 64.91 B C ATOM 2177 CD GLU B 85 −6.257 21.974 35.910 1.00 68.91 B C ATOM 2178 OE1 GLU B 85 −6.095 20.834 36.405 1.00 65.55 B O ATOM 2179 OE2 GLU B 85 −6.862 22.899 36.499 1.00 65.89 B O ATOM 2180 C GLU B 85 −1.864 22.337 35.199 1.00 66.58 B C ATOM 2181 O GLU B 85 −0.923 23.040 34.844 1.00 66.29 B O ATOM 2182 N LEU B 86 −1.711 21.079 35.597 1.00 62.57 B N ATOM 2183 CA LEU B 86 −0.455 20.359 35.478 1.00 60.61 B C ATOM 2184 CB LEU B 86 −0.009 19.849 36.847 1.00 60.27 B C ATOM 2185 CG LEU B 86 1.439 19.435 37.129 1.00 60.52 B C ATOM 2186 CD1 LEU B 86 2.416 20.381 36.467 1.00 61.87 B C ATOM 2187 CD2 LEU B 86 1.696 18.008 36.690 1.00 64.51 B C ATOM 2188 C LEU B 86 −0.737 19.200 34.535 1.00 63.39 B C ATOM 2189 O LEU B 86 −0.506 18.037 34.861 1.00 65.16 B O ATOM 2190 N ASP B 87 −1.256 19.537 33.359 1.00 61.64 B N ATOM 2191 CA ASP B 87 −1.770 18.542 32.429 1.00 61.56 B C ATOM 2192 CB ASP B 87 −2.658 19.199 31.371 1.00 65.92 B C ATOM 2193 CG ASP B 87 −2.119 20.538 30.902 1.00 66.43 B C ATOM 2194 OD1 ASP B 87 −1.771 20.640 29.702 1.00 68.19 B O ATOM 2195 OD2 ASP B 87 −2.053 21.480 31.729 1.00 63.74 B O ATOM 2196 C ASP B 87 −0.688 17.744 31.737 1.00 64.47 B C ATOM 2197 O ASP B 87 0.489 17.864 32.049 1.00 65.31 B O ATOM 2198 N SER B 88 −1.105 16.928 30.780 1.00 63.17 B N ATOM 2199 CA SER B 88 −0.168 16.115 30.044 1.00 62.88 B C ATOM 2200 CB SER B 88 −0.904 15.192 29.075 1.00 67.00 B C ATOM 2201 OG SER B 88 −0.027 14.214 28.543 1.00 72.17 B O ATOM 2202 C SER B 88 0.825 17.000 29.297 1.00 66.18 B C ATOM 2203 O SER B 88 2.032 16.910 29.516 1.00 64.60 B O ATOM 2204 N ALA B 89 0.322 17.861 28.421 1.00 62.37 B N ATOM 2205 CA ALA B 89 1.207 18.666 27.589 1.00 63.00 B C ATOM 2206 CB ALA B 89 0.403 19.591 26.690 1.00 64.46 B C ATOM 2207 C ALA B 89 2.189 19.460 28.444 1.00 61.89 B C ATOM 2208 O ALA B 89 3.393 19.508 28.166 1.00 62.14 B O ATOM 2209 N THR B 90 1.673 20.071 29.498 1.00 58.56 B N ATOM 2210 CA THR B 90 2.496 20.895 30.363 1.00 55.92 B C ATOM 2211 CB THR B 90 1.623 21.644 31.390 1.00 56.32 B C ATOM 2212 OG1 THR B 90 0.735 22.539 30.700 1.00 60.70 B O ATOM 2213 CG2 THR B 90 2.470 22.436 32.354 1.00 54.76 B C ATOM 2214 C THR B 90 3.548 20.040 31.057 1.00 55.44 B C ATOM 2215 O THR B 90 4.555 20.545 31.540 1.00 54.24 B O ATOM 2216 N LEU B 91 3.317 18.733 31.074 1.00 57.13 B N ATOM 2217 CA LEU B 91 4.183 17.796 31.781 1.00 57.20 B C ATOM 2218 CB LEU B 91 3.326 16.688 32.402 1.00 60.86 B C ATOM 2219 CG LEU B 91 3.697 16.121 33.775 1.00 61.80 B C ATOM 2220 CD1 LEU B 91 4.118 17.229 34.706 1.00 61.04 B C ATOM 2221 CD2 LEU B 91 2.531 15.335 34.374 1.00 62.79 B C ATOM 2222 C LEU B 91 5.246 17.207 30.834 1.00 54.07 B C ATOM 2223 O LEU B 91 6.413 17.035 31.200 1.00 49.01 B O ATOM 2224 N LYS B 92 4.834 16.896 29.610 1.00 55.13 B N ATOM 2225 CA LYS B 92 5.795 16.529 28.583 1.00 58.62 B C ATOM 2226 CB LYS B 92 5.094 16.299 27.239 1.00 56.97 B C ATOM 2227 CG LYS B 92 6.013 15.851 26.100 1.00 58.61 B C ATOM 2228 CD LYS B 92 5.333 16.040 24.735 1.00 60.82 B C ATOM 2229 CE LYS B 92 6.324 16.044 23.570 1.00 59.76 B C ATOM 2230 NZ LYS B 92 7.265 17.209 23.604 1.00 59.11 B N ATOM 2231 C LYS B 92 6.832 17.657 28.491 1.00 52.92 B C ATOM 2232 O LYS B 92 8.037 17.401 28.499 1.00 54.82 B O ATOM 2233 N ALA B 93 6.349 18.898 28.446 1.00 47.56 B N ATOM 2234 CA ALA B 93 7.199 20.076 28.376 1.00 45.69 B C ATOM 2235 CB ALA B 93 6.359 21.333 28.533 1.00 48.59 B C ATOM 2236 C ALA B 93 8.303 20.047 29.429 1.00 50.95 B C ATOM 2237 O ALA B 93 9.500 20.085 29.105 1.00 50.16 B O ATOM 2238 N MET B 94 7.893 19.988 30.691 1.00 49.16 B N ATOM 2239 CA MET B 94 8.820 19.986 31.817 1.00 46.96 B C ATOM 2240 CB MET B 94 8.056 19.991 33.146 1.00 45.86 B C ATOM 2241 CG MET B 94 7.453 21.338 33.536 1.00 54.49 B C ATOM 2242 SD MET B 94 6.100 21.201 34.749 1.00 56.31 B S ATOM 2243 CE MET B 94 6.440 22.596 35.824 1.00 45.62 B C ATOM 2244 C MET B 94 9.815 18.821 31.790 1.00 47.82 B C ATOM 2245 O MET B 94 10.853 18.882 32.450 1.00 46.72 B O ATOM 2246 N ARG B 95 9.501 17.764 31.041 1.00 45.03 B N ATOM 2247 CA ARG B 95 10.415 16.626 30.920 1.00 44.41 B C ATOM 2248 CB ARG B 95 9.643 15.310 30.780 1.00 52.40 B C ATOM 2249 CG ARG B 95 9.744 14.393 32.000 1.00 54.06 B C ATOM 2250 CD ARG B 95 8.447 13.649 32.232 1.00 51.63 B C ATOM 2251 NE ARG B 95 7.745 13.408 30.979 1.00 55.01 B N ATOM 2252 CZ ARG B 95 6.564 12.805 30.894 1.00 62.66 B C ATOM 2253 NH1 ARG B 95 5.957 12.376 31.998 1.00 58.00 B N ATOM 2254 NH2 ARG B 95 5.992 12.625 29.704 1.00 59.92 B N ATOM 2255 C ARG B 95 11.418 16.755 29.774 1.00 44.64 B C ATOM 2256 O ARG B 95 12.330 15.938 29.652 1.00 41.99 B O ATOM 2257 N THR B 96 11.242 17.764 28.929 1.00 37.49 B N ATOM 2258 CA THR B 96 12.109 17.918 27.781 1.00 40.66 B C ATOM 2259 CB THR B 96 11.421 18.679 26.644 1.00 41.09 B C ATOM 2260 OG1 THR B 96 10.229 17.979 26.272 1.00 48.42 B O ATOM 2261 CG2 THR B 96 12.318 18.742 25.425 1.00 41.04 B C ATOM 2262 C THR B 96 13.430 18.573 28.173 1.00 38.47 B C ATOM 2263 O THR B 96 13.455 19.581 28.887 1.00 37.15 B O ATOM 2264 N PRO B 97 14.544 17.977 27.722 1.00 41.30 B N ATOM 2265 CD PRO B 97 14.609 16.741 26.934 1.00 37.26 B C ATOM 2266 CA PRO B 97 15.864 18.582 27.902 1.00 32.37 B C ATOM 2267 CB PRO B 97 16.752 17.701 27.038 1.00 39.42 B C ATOM 2268 CG PRO B 97 16.039 16.382 27.030 1.00 44.04 B C ATOM 2269 C PRO B 97 15.821 20.000 27.357 1.00 31.26 B C ATOM 2270 O PRO B 97 15.135 20.244 26.371 1.00 33.06 B O ATOM 2271 N ARG B 98 16.530 20.927 27.986 1.00 34.30 B N ATOM 2272 CA ARG B 98 16.362 22.322 27.649 1.00 30.20 B C ATOM 2273 CB ARG B 98 15.155 22.862 28.396 1.00 34.40 B C ATOM 2274 CG ARG B 98 15.544 23.357 29.782 1.00 35.93 B C ATOM 2275 CD ARG B 98 14.373 23.612 30.695 1.00 37.63 B C ATOM 2276 NE ARG B 98 13.403 24.596 30.218 1.00 39.37 B N ATOM 2277 CZ ARG B 98 13.571 25.918 30.221 1.00 38.21 B C ATOM 2278 NH1 ARG B 98 12.594 26.699 29.806 1.00 34.09 B N ATOM 2279 NH2 ARG B 98 14.709 26.461 30.612 1.00 37.91 B N ATOM 2280 C ARG B 98 17.584 23.142 28.056 1.00 33.56 B C ATOM 2281 O ARG B 98 18.464 22.657 28.769 1.00 33.78 B O ATOM 2282 N CYS B 99 17.609 24.404 27.631 1.00 32.32 B N ATOM 2283 CA CYS B 99 18.677 25.310 28.017 1.00 29.79 B C ATOM 2284 CB CYS B 99 18.662 26.576 27.139 1.00 25.97 B C ATOM 2285 SG CYS B 99 19.716 27.860 27.793 1.00 30.26 B S ATOM 2286 C CYS B 99 18.533 25.649 29.500 1.00 36.85 B C ATOM 2287 O CYS B 99 17.427 25.843 30.000 1.00 40.02 B O ATOM 2288 N GLY B 100 19.646 25.724 30.213 1.00 31.95 B N ATOM 2289 CA GLY B 100 19.602 25.975 31.640 1.00 37.37 B C ATOM 2290 C GLY B 100 19.406 27.427 32.037 1.00 37.12 B C ATOM 2291 O GLY B 100 19.360 27.744 33.222 1.00 36.76 B O ATOM 2292 N VAL B 101 19.317 28.323 31.061 1.00 35.23 B N ATOM 2293 CA VAL B 101 19.163 29.733 31.389 1.00 38.21 B C ATOM 2294 CB VAL B 101 19.641 30.620 30.233 1.00 33.41 B C ATOM 2295 CG1 VAL B 101 19.398 32.095 30.526 1.00 34.44 B C ATOM 2296 CG2 VAL B 101 21.123 30.387 29.976 1.00 35.63 B C ATOM 2297 C VAL B 101 17.696 30.034 31.768 1.00 35.02 B C ATOM 2298 O VAL B 101 16.779 29.555 31.117 1.00 31.26 B O ATOM 2299 N PRO B 102 17.485 30.798 32.845 1.00 35.27 B N ATOM 2300 CA PRO B 102 16.121 31.112 33.291 1.00 39.50 B C ATOM 2301 C PRO B 102 15.288 31.771 32.208 1.00 40.68 B C ATOM 2302 CB PRO B 102 16.351 32.076 34.456 1.00 39.74 B C ATOM 2303 CG PRO B 102 17.670 31.628 35.047 1.00 43.17 B C ATOM 2304 CD PRO B 102 18.501 31.207 33.836 1.00 41.03 B C ATOM 2305 O PRO B 102 15.811 32.558 31.429 1.00 40.54 B O ATOM 2306 N ASP B 103 14.008 31.422 32.145 1.00 36.84 B N ATOM 2307 CA ASP B 103 13.083 32.068 31.216 1.00 39.42 B C ATOM 2308 C ASP B 103 12.660 33.443 31.725 1.00 36.78 B C ATOM 2309 CB ASP B 103 11.851 31.193 30.996 1.00 37.22 B C ATOM 2310 CG ASP B 103 12.208 29.807 30.507 1.00 42.54 B C ATOM 2311 OD1 ASP B 103 13.074 29.716 29.619 1.00 37.92 B O ATOM 2312 OD2 ASP B 103 11.638 28.810 31.009 1.00 36.72 B O ATOM 2313 O ASP B 103 12.338 34.335 30.942 1.00 31.02 B O ATOM 2314 N LEU B 104 12.650 33.597 33.047 1.00 44.87 B N ATOM 2315 CA LEU B 104 12.336 34.881 33.680 1.00 48.54 B C ATOM 2316 C LEU B 104 13.281 35.151 34.848 1.00 42.34 B C ATOM 2317 CB LEU B 104 10.884 34.908 34.176 1.00 49.26 B C ATOM 2318 CG LEU B 104 9.764 34.533 33.201 1.00 48.04 B C ATOM 2319 CD1 LEU B 104 8.467 34.213 33.956 1.00 47.38 B C ATOM 2320 CD2 LEU B 104 9.532 35.624 32.167 1.00 42.58 B C ATOM 2321 O LEU B 104 13.403 36.286 35.311 1.00 41.60 B O ATOM 2322 N VAL B 109 22.008 39.187 39.070 1.00 45.74 B N ATOM 2323 CA VAL B 109 22.331 40.533 38.609 1.00 52.19 B C ATOM 2324 C VAL B 109 23.699 40.598 37.934 1.00 55.61 B C ATOM 2325 CB VAL B 109 22.264 41.571 39.749 1.00 56.64 B C ATOM 2326 CG1 VAL B 109 23.101 42.794 39.393 1.00 50.47 B C ATOM 2327 CG2 VAL B 109 22.724 40.955 41.073 1.00 57.06 B C ATOM 2328 O VAL B 109 24.692 40.098 38.466 1.00 52.03 B O ATOM 2329 N PHE B 110 23.732 41.214 36.755 1.00 55.16 B N ATOM 2330 CA PHE B 110 24.940 41.285 35.936 1.00 50.88 B C ATOM 2331 C PHE B 110 25.427 42.699 35.806 1.00 52.10 B C ATOM 2332 CB PHE B 110 24.670 40.755 34.540 1.00 43.64 B C ATOM 2333 CG PHE B 110 24.383 39.310 34.517 1.00 44.34 B C ATOM 2334 CD1 PHE B 110 25.360 38.405 34.874 1.00 46.49 B C ATOM 2335 CD2 PHE B 110 23.138 38.849 34.175 1.00 47.06 B C ATOM 2336 CE1 PHE B 110 25.105 37.059 34.876 1.00 46.52 B C ATOM 2337 CE2 PHE B 110 22.879 37.504 34.176 1.00 49.10 B C ATOM 2338 CZ PHE B 110 23.870 36.608 34.527 1.00 43.61 B C ATOM 2339 O PHE B 110 24.817 43.631 36.337 1.00 53.58 B O ATOM 2340 N GLU B 111 26.511 42.864 35.062 1.00 48.54 B N ATOM 2341 CA GLU B 111 27.093 44.180 34.919 1.00 46.97 B C ATOM 2342 CB GLU B 111 28.569 44.155 35.305 1.00 48.79 B C ATOM 2343 CG GLU B 111 29.137 45.507 35.687 1.00 55.89 B C ATOM 2344 CD GLU B 111 30.622 45.431 36.052 1.00 69.12 B C ATOM 2345 OE1 GLU B 111 31.026 44.445 36.710 1.00 64.56 B O ATOM 2346 OE2 GLU B 111 31.383 46.358 35.680 1.00 69.29 B O ATOM 2347 C GLU B 111 26.888 44.768 33.532 1.00 49.19 B C ATOM 2348 O GLU B 111 27.020 44.092 32.508 1.00 49.50 B O ATOM 2349 N GLY B 112 26.516 46.040 33.526 1.00 52.86 B N ATOM 2350 CA GLY B 112 26.493 46.829 32.316 1.00 48.52 B C ATOM 2351 C GLY B 112 25.278 46.701 31.425 1.00 48.74 B C ATOM 2352 O GLY B 112 24.242 46.154 31.790 1.00 40.11 B O ATOM 2353 N ASP B 113 25.458 47.213 30.215 1.00 50.85 B N ATOM 2354 CA ASP B 113 24.442 47.323 29.187 1.00 45.47 B C ATOM 2355 CB ASP B 113 25.071 48.097 28.035 1.00 43.86 B C ATOM 2356 CG ASP B 113 24.055 48.727 27.147 1.00 49.66 B C ATOM 2357 OD1 ASP B 113 22.980 48.121 26.953 1.00 54.15 B O ATOM 2358 OD2 ASP B 113 24.331 49.833 26.636 1.00 53.69 B O ATOM 2359 C ASP B 113 23.894 45.979 28.666 1.00 41.91 B C ATOM 2360 O ASP B 113 22.840 45.939 28.032 1.00 34.00 B O ATOM 2361 N LEU B 114 24.626 44.895 28.918 1.00 40.10 B N ATOM 2362 CA LEU B 114 24.281 43.550 28.430 1.00 41.53 B C ATOM 2363 CB LEU B 114 22.955 43.050 29.021 1.00 45.57 B C ATOM 2364 CG LEU B 114 22.843 42.933 30.547 1.00 43.84 B C ATOM 2365 CD1 LEU B 114 21.670 42.018 30.913 1.00 48.45 B C ATOM 2366 CD2 LEU B 114 24.128 42.425 31.169 1.00 42.72 B C ATOM 2367 C LEU B 114 24.268 43.413 26.902 1.00 41.02 B C ATOM 2368 O LEU B 114 23.618 42.514 26.359 1.00 41.54 B O ATOM 2369 N LYS B 115 24.973 44.332 26.238 1.00 43.71 B N ATOM 2370 CA LYS B 115 25.375 44.254 24.824 1.00 41.78 B C ATOM 2371 CB LYS B 115 24.869 45.484 24.073 1.00 39.99 B C ATOM 2372 CG LYS B 115 23.562 45.328 23.356 1.00 41.16 B C ATOM 2373 CD LYS B 115 22.989 46.706 22.987 1.00 46.05 B C ATOM 2374 CE LYS B 115 24.022 47.624 22.348 1.00 44.60 B C ATOM 2375 NZ LYS B 115 23.891 47.743 20.860 1.00 40.73 B N ATOM 2376 C LYS B 115 26.916 44.264 24.730 1.00 40.31 B C ATOM 2377 O LYS B 115 27.602 44.652 25.685 1.00 37.72 B O ATOM 2378 N TRP B 116 27.454 43.850 23.580 1.00 37.67 B N ATOM 2379 CA TRP B 116 28.865 44.086 23.262 1.00 35.96 B C ATOM 2380 CB TRP B 116 29.353 43.077 22.214 1.00 29.76 B C ATOM 2381 CG TRP B 116 29.391 41.695 22.762 1.00 27.68 B C ATOM 2382 CD2 TRP B 116 30.206 41.228 23.839 1.00 26.56 B C ATOM 2383 CE2 TRP B 116 29.893 39.873 24.040 1.00 28.20 B C ATOM 2384 CE3 TRP B 116 31.175 41.822 24.646 1.00 28.86 B C ATOM 2385 CD1 TRP B 116 28.635 40.636 22.364 1.00 27.78 B C ATOM 2386 NE1 TRP B 116 28.929 39.536 23.127 1.00 30.44 B N ATOM 2387 CZ2 TRP B 116 30.511 39.101 25.015 1.00 29.79 B C ATOM 2388 CZ3 TRP B 116 31.785 41.053 25.608 1.00 34.12 B C ATOM 2389 CH2 TRP B 116 31.453 39.704 25.784 1.00 31.09 B C ATOM 2390 C TRP B 116 29.029 45.495 22.718 1.00 33.35 B C ATOM 2391 O TRP B 116 28.212 45.937 21.927 1.00 32.94 B O ATOM 2392 N HIS B 117 30.089 46.190 23.113 1.00 39.27 B N ATOM 2393 CA HIS B 117 30.341 47.528 22.569 1.00 39.86 B C ATOM 2394 CB HIS B 117 30.302 48.566 23.684 1.00 40.72 B C ATOM 2395 CG HIS B 117 28.932 48.762 24.245 1.00 44.42 B C ATOM 2396 CD2 HIS B 117 27.849 49.403 23.743 1.00 45.91 B C ATOM 2397 ND1 HIS B 117 28.530 48.199 25.438 1.00 48.45 B N ATOM 2398 CE1 HIS B 117 27.265 48.514 25.664 1.00 47.33 B C ATOM 2399 NE2 HIS B 117 26.829 49.243 24.650 1.00 48.08 B N ATOM 2400 C HIS B 117 31.601 47.692 21.690 1.00 45.47 B C ATOM 2401 O HIS B 117 32.283 48.734 21.737 1.00 34.01 B O ATOM 2402 N HIS B 118 31.867 46.676 20.869 1.00 38.19 B N ATOM 2403 CA HIS B 118 32.989 46.667 19.936 1.00 39.90 B C ATOM 2404 CB HIS B 118 34.305 46.463 20.687 1.00 40.02 B C ATOM 2405 CG HIS B 118 34.370 45.178 21.455 1.00 41.12 B C ATOM 2406 CD2 HIS B 118 34.645 43.915 21.055 1.00 38.22 B C ATOM 2407 ND1 HIS B 118 34.133 45.106 22.813 1.00 40.38 B N ATOM 2408 CE1 HIS B 118 34.260 43.853 23.216 1.00 39.36 B C ATOM 2409 NE2 HIS B 118 34.574 43.111 22.168 1.00 38.13 B N ATOM 2410 C HIS B 118 32.742 45.523 18.953 1.00 38.80 B C ATOM 2411 O HIS B 118 32.082 44.563 19.298 1.00 37.79 B O ATOM 2412 N HIS B 119 33.265 45.608 17.738 1.00 39.43 B N ATOM 2413 CA HIS B 119 32.796 44.720 16.669 1.00 38.70 B C ATOM 2414 CB HIS B 119 32.924 45.409 15.308 1.00 45.75 B C ATOM 2415 CG HIS B 119 34.154 46.260 15.174 1.00 57.55 B C ATOM 2416 CD2 HIS B 119 34.578 47.333 15.887 1.00 56.67 B C ATOM 2417 ND1 HIS B 119 35.115 46.041 14.207 1.00 60.13 B N ATOM 2418 CE1 HIS B 119 36.075 46.943 14.330 1.00 61.35 B C ATOM 2419 NE2 HIS B 119 35.776 47.736 15.345 1.00 61.01 B N ATOM 2420 C HIS B 119 33.440 43.332 16.616 1.00 36.49 B C ATOM 2421 O HIS B 119 32.850 42.380 16.095 1.00 30.07 B O ATOM 2422 N ASN B 120 34.657 43.203 17.125 1.00 41.60 B N ATOM 2423 CA ASN B 120 35.355 41.931 16.949 1.00 39.10 B C ATOM 2424 CB ASN B 120 36.772 42.093 16.388 1.00 42.04 B C ATOM 2425 CG ASN B 120 37.470 40.741 16.175 1.00 44.33 B C ATOM 2426 OD1 ASN B 120 36.899 39.807 15.576 1.00 36.73 B O ATOM 2427 ND2 ASN B 120 38.706 40.630 16.677 1.00 46.50 B N ATOM 2428 C ASN B 120 35.362 41.096 18.203 1.00 35.56 B C ATOM 2429 O ASN B 120 36.104 41.357 19.149 1.00 33.58 B O ATOM 2430 N ILE B 121 34.549 40.053 18.191 1.00 32.05 B N ATOM 2431 CA ILE B 121 34.357 39.308 19.415 1.00 33.64 B C ATOM 2432 CB ILE B 121 32.877 38.874 19.601 1.00 31.41 B C ATOM 2433 CG2 ILE B 121 32.687 38.297 20.985 1.00 26.58 B C ATOM 2434 CG1 ILE B 121 31.959 40.067 19.374 1.00 26.86 B C ATOM 2435 CD1 ILE B 121 32.202 41.223 20.384 1.00 32.55 B C ATOM 2436 C ILE B 121 35.271 38.122 19.420 1.00 26.01 B C ATOM 2437 O ILE B 121 35.263 37.334 18.488 1.00 33.42 B O ATOM 2438 N THR B 122 36.056 37.993 20.476 1.00 29.39 B N ATOM 2439 CA THR B 122 37.045 36.922 20.549 1.00 31.05 B C ATOM 2440 CB THR B 122 38.384 37.439 21.087 1.00 34.89 B C ATOM 2441 OG1 THR B 122 38.229 37.876 22.445 1.00 32.45 B O ATOM 2442 CG2 THR B 122 38.903 38.605 20.217 1.00 35.85 B C ATOM 2443 C THR B 122 36.584 35.812 21.464 1.00 32.51 B C ATOM 2444 O THR B 122 36.083 36.073 22.561 1.00 33.63 B O ATOM 2445 N TYR B 123 36.784 34.573 21.035 1.00 33.68 B N ATOM 2446 CA TYR B 123 36.412 33.424 21.851 1.00 34.92 B C ATOM 2447 CB TYR B 123 35.156 32.783 21.273 1.00 28.78 B C ATOM 2448 CG TYR B 123 35.310 32.067 19.945 1.00 26.40 B C ATOM 2449 CD1 TYR B 123 35.170 32.737 18.738 1.00 23.69 B C ATOM 2450 CE1 TYR B 123 35.278 32.067 17.534 1.00 25.64 B C ATOM 2451 CD2 TYR B 123 35.549 30.701 19.912 1.00 31.15 B C ATOM 2452 CE2 TYR B 123 35.666 30.014 18.715 1.00 29.96 B C ATOM 2453 CZ TYR B 123 35.531 30.695 17.538 1.00 33.85 B C ATOM 2454 OH TYR B 123 35.630 29.976 16.376 1.00 29.81 B O ATOM 2455 C TYR B 123 37.507 32.364 22.073 1.00 34.86 B C ATOM 2456 O TYR B 123 38.266 32.044 21.170 1.00 33.65 B O ATOM 2457 N TRP B 124 37.554 31.803 23.278 1.00 38.28 B N ATOM 2458 CA TRP B 124 38.542 30.787 23.624 1.00 35.70 B C ATOM 2459 CB TRP B 124 39.401 31.293 24.782 1.00 40.41 B C ATOM 2460 CG TRP B 124 40.420 30.312 25.249 1.00 39.86 B C ATOM 2461 CD2 TRP B 124 40.850 30.103 26.597 1.00 44.32 B C ATOM 2462 CE2 TRP B 124 41.835 29.096 26.569 1.00 40.40 B C ATOM 2463 CE3 TRP B 124 40.496 30.670 27.828 1.00 45.84 B C ATOM 2464 CD1 TRP B 124 41.142 29.451 24.477 1.00 40.68 B C ATOM 2465 NE1 TRP B 124 41.992 28.712 25.265 1.00 42.22 B N ATOM 2466 CZ2 TRP B 124 42.467 28.636 27.725 1.00 44.51 B C ATOM 2467 CZ3 TRP B 124 41.123 30.220 28.973 1.00 47.21 B C ATOM 2468 CH2 TRP B 124 42.100 29.210 28.914 1.00 50.81 B C ATOM 2469 C TRP B 124 37.945 29.425 23.981 1.00 41.05 B C ATOM 2470 O TRP B 124 37.325 29.270 25.026 1.00 44.41 B O ATOM 2471 N ILE B 125 38.149 28.431 23.122 1.00 37.85 B N ATOM 2472 CA ILE B 125 37.737 27.068 23.419 1.00 34.16 B C ATOM 2473 CB ILE B 125 37.859 26.197 22.186 1.00 36.18 B C ATOM 2474 CG2 ILE B 125 37.370 24.786 22.469 1.00 41.36 B C ATOM 2475 CG1 ILE B 125 37.111 26.846 21.029 1.00 32.68 B C ATOM 2476 CD1 ILE B 125 36.908 25.944 19.856 1.00 37.45 B C ATOM 2477 C ILE B 125 38.621 26.484 24.486 1.00 42.02 B C ATOM 2478 O ILE B 125 39.591 25.799 24.181 1.00 44.71 B O ATOM 2479 N GLN B 126 38.274 26.749 25.740 1.00 42.74 B N ATOM 2480 CA GLN B 126 39.124 26.447 26.882 1.00 40.60 B C ATOM 2481 CB GLN B 126 38.487 27.000 28.158 1.00 42.12 B C ATOM 2482 CG GLN B 126 39.413 27.042 29.346 1.00 46.23 B C ATOM 2483 CD GLN B 126 38.727 27.578 30.596 1.00 56.73 B C ATOM 2484 OE1 GLN B 126 37.949 26.871 31.253 1.00 56.80 B O ATOM 2485 NE2 GLN B 126 39.019 28.836 30.937 1.00 53.02 B N ATOM 2486 C GLN B 126 39.433 24.968 27.070 1.00 41.42 B C ATOM 2487 O GLN B 126 40.489 24.623 27.579 1.00 45.51 B O ATOM 2488 N ASN B 127 38.499 24.100 26.711 1.00 40.04 B N ATOM 2489 CA ASN B 127 38.713 22.651 26.812 1.00 40.78 B C ATOM 2490 CB ASN B 127 38.693 22.133 28.267 1.00 41.99 B C ATOM 2491 CG ASN B 127 37.336 22.289 28.953 1.00 45.31 B C ATOM 2492 OD1 ASN B 127 36.324 22.570 28.320 1.00 40.92 B O ATOM 2493 ND2 ASN B 127 37.321 22.091 30.263 1.00 38.46 B N ATOM 2494 C ASN B 127 37.769 21.890 25.886 1.00 39.75 B C ATOM 2495 O ASN B 127 36.944 22.522 25.232 1.00 39.13 B O ATOM 2496 N TYR B 128 37.934 20.565 25.780 1.00 41.63 B N ATOM 2497 CA TYR B 128 37.200 19.743 24.799 1.00 39.72 B C ATOM 2498 CB TYR B 128 38.128 19.246 23.688 1.00 41.35 B C ATOM 2499 CG TYR B 128 38.617 20.315 22.748 1.00 43.51 B C ATOM 2500 CD1 TYR B 128 38.046 20.478 21.501 1.00 38.99 B C ATOM 2501 CE1 TYR B 128 38.494 21.453 20.644 1.00 41.32 B C ATOM 2502 CD2 TYR B 128 39.659 21.154 23.111 1.00 46.44 B C ATOM 2503 CE2 TYR B 128 40.111 22.128 22.263 1.00 42.42 B C ATOM 2504 CZ TYR B 128 39.528 22.268 21.034 1.00 40.18 B C ATOM 2505 OH TYR B 128 39.987 23.238 20.184 1.00 48.91 B O ATOM 2506 C TYR B 128 36.593 18.508 25.428 1.00 43.39 B C ATOM 2507 O TYR B 128 37.197 17.906 26.317 1.00 47.74 B O ATOM 2508 N SER B 129 35.425 18.109 24.934 1.00 41.54 B N ATOM 2509 CA SER B 129 34.770 16.896 25.403 1.00 42.63 B C ATOM 2510 CB SER B 129 33.251 17.013 25.214 1.00 38.24 B C ATOM 2511 OG SER B 129 32.690 15.778 24.798 1.00 40.30 B O ATOM 2512 C SER B 129 35.298 15.690 24.638 1.00 40.68 B C ATOM 2513 O SER B 129 35.601 15.783 23.458 1.00 39.80 B O ATOM 2514 N GLU B 130 35.378 14.546 25.306 1.00 46.04 B N ATOM 2515 CA GLU B 130 35.923 13.343 24.681 1.00 43.54 B C ATOM 2516 CB GLU B 130 36.183 12.256 25.729 1.00 46.66 B C ATOM 2517 CG GLU B 130 37.410 12.505 26.599 1.00 48.87 B C ATOM 2518 CD GLU B 130 38.697 12.625 25.785 1.00 56.90 B C ATOM 2519 OE1 GLU B 130 38.981 11.713 24.977 1.00 64.25 B O ATOM 2520 OE2 GLU B 130 39.430 13.628 25.958 1.00 57.04 B O ATOM 2521 C GLU B 130 35.036 12.784 23.580 1.00 44.55 B C ATOM 2522 O GLU B 130 35.470 11.935 22.790 1.00 48.00 B O ATOM 2523 N ASP B 131 33.802 13.261 23.513 1.00 42.33 B N ATOM 2524 CA ASP B 131 32.802 12.604 22.679 1.00 38.51 B C ATOM 2525 CB ASP B 131 31.395 13.020 23.110 1.00 45.73 B C ATOM 2526 CG ASP B 131 31.133 12.723 24.577 1.00 45.01 B C ATOM 2527 OD1 ASP B 131 31.554 11.635 25.050 1.00 43.17 B O ATOM 2528 OD2 ASP B 131 30.526 13.580 25.256 1.00 47.36 B O ATOM 2529 C ASP B 131 32.993 12.798 21.182 1.00 44.35 B C ATOM 2530 O ASP B 131 32.362 12.093 20.383 1.00 44.17 B O ATOM 2531 N LEU B 132 33.865 13.739 20.810 1.00 40.28 B N ATOM 2532 CA LEU B 132 34.128 14.063 19.405 1.00 38.93 B C ATOM 2533 CB LEU B 132 33.193 15.177 18.934 1.00 40.27 B C ATOM 2534 CG LEU B 132 31.675 14.957 18.881 1.00 38.56 B C ATOM 2535 CD1 LEU B 132 30.947 16.213 19.275 1.00 35.37 B C ATOM 2536 CD2 LEU B 132 31.224 14.514 17.517 1.00 34.79 B C ATOM 2537 C LEU B 132 35.577 14.522 19.194 1.00 42.01 B C ATOM 2538 O LEU B 132 36.236 14.987 20.137 1.00 36.91 B O ATOM 2539 N PRO B 133 36.073 14.408 17.945 1.00 40.13 B N ATOM 2540 CD PRO B 133 35.467 13.656 16.833 1.00 37.38 B C ATOM 2541 CA PRO B 133 37.388 14.957 17.587 1.00 36.50 B C ATOM 2542 CB PRO B 133 37.469 14.688 16.085 1.00 37.78 B C ATOM 2543 CG PRO B 133 36.613 13.461 15.884 1.00 41.15 B C ATOM 2544 C PRO B 133 37.457 16.464 17.863 1.00 41.04 B C ATOM 2545 O PRO B 133 36.484 17.184 17.629 1.00 41.40 B O ATOM 2546 N ARG B 134 38.598 16.926 18.355 1.00 34.23 B N ATOM 2547 CA ARG B 134 38.801 18.329 18.673 1.00 36.89 B C ATOM 2548 CB ARG B 134 40.243 18.565 19.135 1.00 37.59 B C ATOM 2549 CG ARG B 134 40.576 17.987 20.478 1.00 38.06 B C ATOM 2550 CD ARG B 134 41.658 18.785 21.146 1.00 40.03 B C ATOM 2551 NE ARG B 134 41.908 18.317 22.505 1.00 45.68 B N ATOM 2552 CZ ARG B 134 42.793 18.866 23.333 1.00 49.76 B C ATOM 2553 NH1 ARG B 134 43.517 19.913 22.945 1.00 56.93 B N ATOM 2554 NH2 ARG B 134 42.948 18.375 24.555 1.00 52.95 B N ATOM 2555 C ARG B 134 38.455 19.305 17.538 1.00 40.52 B C ATOM 2556 O ARG B 134 38.081 20.454 17.806 1.00 38.77 B O ATOM 2557 N ALA B 135 38.594 18.867 16.286 1.00 40.56 B N ATOM 2558 CA ALA B 135 38.337 19.746 15.146 1.00 39.73 B C ATOM 2559 CB ALA B 135 39.242 19.389 13.993 1.00 39.64 B C ATOM 2560 C ALA B 135 36.872 19.686 14.703 1.00 38.66 B C ATOM 2561 O ALA B 135 36.360 20.583 14.024 1.00 36.34 B O ATOM 2562 N VAL B 136 36.206 18.601 15.045 1.00 35.13 B N ATOM 2563 CA VAL B 136 34.779 18.532 14.784 1.00 36.49 B C ATOM 2564 CB VAL B 136 34.297 17.089 14.899 1.00 35.30 B C ATOM 2565 CG1 VAL B 136 32.801 16.998 14.689 1.00 35.19 B C ATOM 2566 CG2 VAL B 136 35.028 16.238 13.863 1.00 31.26 B C ATOM 2567 C VAL B 136 34.095 19.513 15.772 1.00 30.51 B C ATOM 2568 O VAL B 136 33.201 20.276 15.416 1.00 33.64 B O ATOM 2569 N ILE B 137 34.597 19.544 16.989 1.00 29.92 B N ATOM 2570 CA ILE B 137 34.167 20.532 17.959 1.00 33.71 B C ATOM 2571 CB ILE B 137 34.764 20.218 19.325 1.00 32.97 B C ATOM 2572 CG2 ILE B 137 34.639 21.401 20.239 1.00 37.27 B C ATOM 2573 CG1 ILE B 137 34.068 18.979 19.921 1.00 36.00 B C ATOM 2574 CD1 ILE B 137 34.770 18.423 21.129 1.00 32.61 B C ATOM 2575 C ILE B 137 34.509 21.963 17.524 1.00 37.21 B C ATOM 2576 O ILE B 137 33.600 22.800 17.344 1.00 34.33 B O ATOM 2577 N ASP B 138 35.808 22.234 17.357 1.00 31.17 B N ATOM 2578 CA ASP B 138 36.296 23.498 16.799 1.00 32.57 B C ATOM 2579 CB ASP B 138 37.703 23.326 16.197 1.00 33.14 B C ATOM 2580 CG ASP B 138 38.758 23.067 17.240 1.00 39.79 B C ATOM 2581 OD1 ASP B 138 38.456 23.245 18.438 1.00 45.17 B O ATOM 2582 OD2 ASP B 138 39.890 22.685 16.863 1.00 46.04 B O ATOM 2583 C ASP B 138 35.402 23.988 15.682 1.00 25.16 B C ATOM 2584 O ASP B 138 35.117 25.179 15.577 1.00 29.98 B O ATOM 2585 N ASP B 139 34.965 23.064 14.837 1.00 27.40 B N ATOM 2586 CA ASP B 139 34.217 23.418 13.636 1.00 28.27 B C ATOM 2587 CB ASP B 139 34.277 22.260 12.650 1.00 29.54 B C ATOM 2588 CG ASP B 139 33.304 22.421 11.514 1.00 33.04 B C ATOM 2589 OD1 ASP B 139 33.534 23.304 10.656 1.00 36.55 B O ATOM 2590 OD2 ASP B 139 32.316 21.655 11.453 1.00 31.94 B O ATOM 2591 C ASP B 139 32.741 23.736 13.934 1.00 33.68 B C ATOM 2592 O ASP B 139 32.113 24.596 13.279 1.00 28.11 B O ATOM 2593 N ALA B 140 32.190 23.021 14.913 1.00 31.25 B N ATOM 2594 CA ALA B 140 30.785 23.214 15.297 1.00 31.70 B C ATOM 2595 CB ALA B 140 30.321 22.089 16.230 1.00 27.54 B C ATOM 2596 C ALA B 140 30.642 24.574 15.963 1.00 23.86 B C ATOM 2597 O ALA B 140 29.762 25.348 15.633 1.00 27.33 B O ATOM 2598 N PHE B 141 31.524 24.875 16.900 1.00 25.73 B N ATOM 2599 CA PHE B 141 31.568 26.228 17.432 1.00 27.06 B C ATOM 2600 CB PHE B 141 32.652 26.366 18.487 1.00 27.20 B C ATOM 2601 CG PHE B 141 32.457 25.479 19.664 1.00 31.72 B C ATOM 2602 CD1 PHE B 141 31.184 25.022 20.003 1.00 32.52 B C ATOM 2603 CD2 PHE B 141 33.539 25.118 20.465 1.00 30.15 B C ATOM 2604 CE1 PHE B 141 31.002 24.204 21.113 1.00 31.73 B C ATOM 2605 CE2 PHE B 141 33.372 24.300 21.574 1.00 33.44 B C ATOM 2606 CZ PHE B 141 32.098 23.841 21.899 1.00 34.20 B C ATOM 2607 C PHE B 141 31.742 27.302 16.345 1.00 33.52 B C ATOM 2608 O PHE B 141 31.188 28.408 16.462 1.00 34.64 B O ATOM 2609 N ALA B 142 32.495 26.994 15.289 1.00 31.95 B N ATOM 2610 CA ALA B 142 32.710 27.984 14.215 1.00 29.67 B C ATOM 2611 CB ALA B 142 33.850 27.524 13.265 1.00 30.45 B C ATOM 2612 C ALA B 142 31.455 28.252 13.409 1.00 24.46 B C ATOM 2613 O ALA B 142 31.068 29.405 13.170 1.00 21.93 B O ATOM 2614 N ARG B 143 30.862 27.172 12.926 1.00 25.94 B N ATOM 2615 CA ARG B 143 29.576 27.232 12.241 1.00 29.70 B C ATOM 2616 CB ARG B 143 29.109 25.828 11.911 1.00 23.86 B C ATOM 2617 CG ARG B 143 29.870 25.200 10.739 1.00 32.24 B C ATOM 2618 CD ARG B 143 29.975 23.700 10.929 1.00 34.53 B C ATOM 2619 NE ARG B 143 28.646 23.151 10.856 1.00 41.14 B N ATOM 2620 CZ ARG B 143 28.192 22.148 11.587 1.00 35.61 B C ATOM 2621 NH1 ARG B 143 28.965 21.533 12.473 1.00 34.83 B N ATOM 2622 NH2 ARG B 143 26.942 21.773 11.414 1.00 37.65 B N ATOM 2623 C ARG B 143 28.518 27.948 13.097 1.00 25.15 B C ATOM 2624 O ARG B 143 27.696 28.710 12.591 1.00 27.67 B O ATOM 2625 N ALA B 144 28.555 27.692 14.391 1.00 22.96 B N ATOM 2626 CA ALA B 144 27.612 28.318 15.279 1.00 28.85 B C ATOM 2627 CB ALA B 144 27.855 27.838 16.699 1.00 26.99 B C ATOM 2628 C ALA B 144 27.742 29.844 15.174 1.00 29.28 B C ATOM 2629 O ALA B 144 26.748 30.553 14.960 1.00 24.56 B O ATOM 2630 N PHE B 145 28.966 30.350 15.308 1.00 23.93 B N ATOM 2631 CA PHE B 145 29.188 31.798 15.233 1.00 27.09 B C ATOM 2632 CB PHE B 145 30.632 32.160 15.597 1.00 23.43 B C ATOM 2633 CG PHE B 145 30.929 32.071 17.047 1.00 25.14 B C ATOM 2634 CD1 PHE B 145 30.432 33.019 17.931 1.00 27.69 B C ATOM 2635 CD2 PHE B 145 31.729 31.060 17.543 1.00 25.48 B C ATOM 2636 CE1 PHE B 145 30.726 32.934 19.289 1.00 23.37 B C ATOM 2637 CE2 PHE B 145 32.044 30.990 18.885 1.00 24.74 B C ATOM 2638 CZ PHE B 145 31.544 31.924 19.759 1.00 26.91 B C ATOM 2639 C PHE B 145 28.855 32.350 13.859 1.00 26.73 B C ATOM 2640 O PHE B 145 28.362 33.482 13.729 1.00 26.48 B O ATOM 2641 N ALA B 146 29.126 31.558 12.822 1.00 28.34 B N ATOM 2642 CA ALA B 146 28.839 32.010 11.468 1.00 24.97 B C ATOM 2643 CB ALA B 146 29.211 30.975 10.489 1.00 24.79 B C ATOM 2644 C ALA B 146 27.368 32.372 11.292 1.00 27.63 B C ATOM 2645 O ALA B 146 27.035 33.248 10.477 1.00 20.89 B O ATOM 2646 N LEU B 147 26.471 31.672 12.001 1.00 29.36 B N ATOM 2647 CA LEU B 147 25.037 32.000 11.883 1.00 20.93 B C ATOM 2648 CB LEU B 147 24.177 31.116 12.787 1.00 27.60 B C ATOM 2649 CG LEU B 147 23.976 29.660 12.369 1.00 26.34 B C ATOM 2650 CD1 LEU B 147 23.644 28.788 13.567 1.00 30.17 B C ATOM 2651 CD2 LEU B 147 22.914 29.520 11.287 1.00 28.65 B C ATOM 2652 C LEU B 147 24.863 33.461 12.277 1.00 15.44 B C ATOM 2653 O LEU B 147 24.330 34.246 11.525 1.00 23.60 B O ATOM 2654 N TRP B 148 25.350 33.813 13.456 1.00 20.89 B N ATOM 2655 CA TRP B 148 25.208 35.149 14.002 1.00 25.33 B C ATOM 2656 CB TRP B 148 25.555 35.119 15.497 1.00 29.18 B C ATOM 2657 CG TRP B 148 24.630 34.219 16.326 1.00 37.59 B C ATOM 2658 CD2 TRP B 148 23.223 34.413 16.571 1.00 29.17 B C ATOM 2659 CE2 TRP B 148 22.781 33.341 17.371 1.00 34.19 B C ATOM 2660 CE3 TRP B 148 22.298 35.390 16.186 1.00 30.19 B C ATOM 2661 CD1 TRP B 148 24.967 33.059 16.979 1.00 37.03 B C ATOM 2662 NE1 TRP B 148 23.859 32.531 17.609 1.00 33.28 B N ATOM 2663 CZ2 TRP B 148 21.447 33.225 17.805 1.00 33.60 B C ATOM 2664 CZ3 TRP B 148 20.968 35.263 16.612 1.00 32.19 B C ATOM 2665 CH2 TRP B 148 20.564 34.189 17.403 1.00 29.62 B C ATOM 2666 C TRP B 148 26.060 36.207 13.278 1.00 29.92 B C ATOM 2667 O TRP B 148 25.779 37.404 13.337 1.00 20.03 B O ATOM 2668 N SER B 149 27.118 35.782 12.590 1.00 32.08 B N ATOM 2669 CA SER B 149 27.994 36.785 12.000 1.00 25.83 B C ATOM 2670 CB SER B 149 29.308 36.163 11.508 1.00 30.48 B C ATOM 2671 OG SER B 149 30.227 37.211 11.257 1.00 35.92 B O ATOM 2672 C SER B 149 27.278 37.441 10.851 1.00 22.19 B C ATOM 2673 O SER B 149 27.379 38.646 10.609 1.00 24.42 B O ATOM 2674 N ALA B 150 26.544 36.630 10.122 1.00 18.70 B N ATOM 2675 CA ALA B 150 25.912 37.099 8.906 1.00 19.08 B C ATOM 2676 CB ALA B 150 25.380 35.906 8.138 1.00 21.25 B C ATOM 2677 C ALA B 150 24.783 38.107 9.146 1.00 26.52 B C ATOM 2678 O ALA B 150 24.435 38.885 8.244 1.00 21.90 B O ATOM 2679 N VAL B 151 24.184 38.069 10.342 1.00 22.69 B N ATOM 2680 CA VAL B 151 22.967 38.856 10.601 1.00 25.66 B C ATOM 2681 CB VAL B 151 21.826 37.970 11.140 1.00 22.60 B C ATOM 2682 CG1 VAL B 151 21.342 37.016 10.079 1.00 20.46 B C ATOM 2683 CG2 VAL B 151 22.273 37.209 12.378 1.00 22.58 B C ATOM 2684 C VAL B 151 23.221 39.981 11.597 1.00 29.63 B C ATOM 2685 O VAL B 151 22.276 40.520 12.176 1.00 29.66 B O ATOM 2686 N THR B 152 24.501 40.309 11.799 1.00 28.93 B N ATOM 2687 CA THR B 152 24.941 41.357 12.717 1.00 29.43 B C ATOM 2688 CB THR B 152 25.256 40.788 14.106 1.00 33.71 B C ATOM 2689 OG1 THR B 152 26.504 40.101 14.062 1.00 33.49 B O ATOM 2690 CG2 THR B 152 24.163 39.817 14.593 1.00 27.41 B C ATOM 2691 C THR B 152 26.237 42.032 12.217 1.00 33.69 B C ATOM 2692 O THR B 152 26.902 41.515 11.317 1.00 30.17 B O ATOM 2693 N PRO B 153 26.577 43.200 12.786 1.00 32.70 B N ATOM 2694 CD PRO B 153 25.618 44.040 13.517 1.00 33.25 B C ATOM 2695 CA PRO B 153 27.803 43.951 12.506 1.00 34.26 B C ATOM 2696 CB PRO B 153 27.469 45.359 13.024 1.00 34.92 B C ATOM 2697 CG PRO B 153 25.997 45.414 13.067 1.00 32.81 B C ATOM 2698 C PRO B 153 29.001 43.426 13.275 1.00 33.52 B C ATOM 2699 O PRO B 153 29.914 44.199 13.547 1.00 34.26 B O ATOM 2700 N LEU B 154 28.989 42.147 13.637 1.00 31.11 B N ATOM 2701 CA LEU B 154 30.037 41.578 14.472 1.00 31.11 B C ATOM 2702 CB LEU B 154 29.406 40.920 15.688 1.00 31.84 B C ATOM 2703 CG LEU B 154 28.482 41.786 16.543 1.00 34.46 B C ATOM 2704 CD1 LEU B 154 27.740 40.913 17.531 1.00 35.26 B C ATOM 2705 CD2 LEU B 154 29.272 42.842 17.271 1.00 27.29 B C ATOM 2706 C LEU B 154 30.829 40.501 13.740 1.00 28.09 B C ATOM 2707 O LEU B 154 30.322 39.902 12.809 1.00 25.88 B O ATOM 2708 N THR B 155 32.050 40.241 14.203 1.00 28.45 B N ATOM 2709 CA THR B 155 32.831 39.116 13.715 1.00 27.19 B C ATOM 2710 CB THR B 155 34.036 39.558 12.864 1.00 28.36 B C ATOM 2711 OG1 THR B 155 34.977 40.242 13.705 1.00 36.24 B O ATOM 2712 CG2 THR B 155 33.598 40.474 11.776 1.00 25.25 B C ATOM 2713 C THR B 155 33.369 38.377 14.898 1.00 25.14 B C ATOM 2714 O THR B 155 33.595 38.947 15.954 1.00 31.29 B O ATOM 2715 N PHE B 156 33.600 37.094 14.710 1.00 23.88 B N ATOM 2716 CA PHE B 156 34.074 36.258 15.781 1.00 24.06 B C ATOM 2717 CB PHE B 156 33.034 35.184 16.049 1.00 26.77 B C ATOM 2718 CG PHE B 156 31.668 35.775 16.357 1.00 26.24 B C ATOM 2719 CD1 PHE B 156 30.754 35.987 15.347 1.00 27.83 B C ATOM 2720 CD2 PHE B 156 31.365 36.206 17.643 1.00 25.27 B C ATOM 2721 CE1 PHE B 156 29.519 36.579 15.615 1.00 29.83 B C ATOM 2722 CE2 PHE B 156 30.129 36.804 17.929 1.00 26.39 B C ATOM 2723 CZ PHE B 156 29.213 36.984 16.921 1.00 28.36 B C ATOM 2724 C PHE B 156 35.433 35.668 15.397 1.00 31.54 B C ATOM 2725 O PHE B 156 35.611 35.127 14.317 1.00 30.27 B O ATOM 2726 N THR B 157 36.375 35.796 16.305 1.00 30.81 B N ATOM 2727 CA THR B 157 37.737 35.414 16.044 1.00 31.27 B C ATOM 2728 CB THR B 157 38.659 36.642 16.147 1.00 31.97 B C ATOM 2729 OG1 THR B 157 38.450 37.504 15.023 1.00 37.50 B O ATOM 2730 CG2 THR B 157 40.110 36.204 16.181 1.00 35.24 B C ATOM 2731 C THR B 157 38.154 34.462 17.128 1.00 26.84 B C ATOM 2732 O THR B 157 38.189 34.828 18.307 1.00 31.93 B O ATOM 2733 N ARG B 158 38.506 33.247 16.746 1.00 33.28 B N ATOM 2734 CA ARG B 158 39.042 32.299 17.718 1.00 33.83 B C ATOM 2735 CB ARG B 158 39.174 30.923 17.064 1.00 29.38 B C ATOM 2736 CG ARG B 158 39.559 29.843 18.025 1.00 32.76 B C ATOM 2737 CD ARG B 158 39.663 28.473 17.356 1.00 32.09 B C ATOM 2738 NE ARG B 158 40.269 27.545 18.304 1.00 31.08 B N ATOM 2739 CZ ARG B 158 40.513 26.260 18.064 1.00 30.48 B C ATOM 2740 NH1 ARG B 158 40.206 25.722 16.888 1.00 30.78 B N ATOM 2741 NH2 ARG B 158 41.062 25.514 19.013 1.00 33.64 B N ATOM 2742 C ARG B 158 40.400 32.767 18.251 1.00 34.81 B C ATOM 2743 O ARG B 158 41.279 33.151 17.466 1.00 38.61 B O ATOM 2744 N VAL B 159 40.578 32.758 19.570 1.00 34.09 B N ATOM 2745 CA VAL B 159 41.900 33.002 20.150 1.00 34.95 B C ATOM 2746 CB VAL B 159 42.018 34.411 20.789 1.00 30.65 B C ATOM 2747 CG1 VAL B 159 41.650 35.492 19.751 1.00 33.82 B C ATOM 2748 CG2 VAL B 159 41.142 34.532 22.032 1.00 38.78 B C ATOM 2749 C VAL B 159 42.369 31.868 21.092 1.00 38.83 B C ATOM 2750 O VAL B 159 41.704 30.831 21.203 1.00 39.69 B O ATOM 2751 N TYR B 160 43.509 32.048 21.758 1.00 35.17 B N ATOM 2752 CA TYR B 160 44.125 30.933 22.484 1.00 34.52 B C ATOM 2753 CB TYR B 160 45.218 30.211 21.627 1.00 34.78 B C ATOM 2754 CG TYR B 160 44.662 29.508 20.385 1.00 29.89 B C ATOM 2755 CD1 TYR B 160 44.311 30.231 19.260 1.00 32.01 B C ATOM 2756 CE1 TYR B 160 43.772 29.619 18.151 1.00 29.18 B C ATOM 2757 CD2 TYR B 160 44.458 28.131 20.357 1.00 27.82 B C ATOM 2758 CE2 TYR B 160 43.925 27.510 19.234 1.00 22.88 B C ATOM 2759 CZ TYR B 160 43.580 28.265 18.148 1.00 28.40 B C ATOM 2760 OH TYR B 160 43.048 27.687 17.024 1.00 33.31 B O ATOM 2761 C TYR B 160 44.639 31.331 23.866 1.00 36.10 B C ATOM 2762 O TYR B 160 45.389 30.588 24.487 1.00 45.76 B O ATOM 2763 N SER B 161 44.232 32.495 24.360 1.00 34.77 B N ATOM 2764 CA SER B 161 44.494 32.854 25.754 1.00 40.41 B C ATOM 2765 CB SER B 161 45.403 34.072 25.832 1.00 37.53 B C ATOM 2766 OG SER B 161 44.716 35.213 25.345 1.00 48.82 B O ATOM 2767 C SER B 161 43.182 33.194 26.477 1.00 42.79 B C ATOM 2768 O SER B 161 42.154 33.396 25.837 1.00 40.86 B O ATOM 2769 N ARG B 162 43.232 33.285 27.805 1.00 43.77 B N ATOM 2770 CA ARG B 162 42.076 33.737 28.598 1.00 50.22 B C ATOM 2771 CB ARG B 162 42.367 33.644 30.100 1.00 51.70 B C ATOM 2772 CG ARG B 162 43.710 34.232 30.543 1.00 56.16 B C ATOM 2773 CD ARG B 162 43.652 35.740 30.775 1.00 60.42 B C ATOM 2774 NE ARG B 162 44.988 36.296 31.010 1.00 63.52 B N ATOM 2775 CZ ARG B 162 45.233 37.502 31.518 1.00 67.95 B C ATOM 2776 NH1 ARG B 162 44.230 38.302 31.866 1.00 71.00 B N ATOM 2777 NH2 ARG B 162 46.489 37.905 31.687 1.00 66.17 B N ATOM 2778 C ARG B 162 41.657 35.154 28.244 1.00 48.43 B C ATOM 2779 O ARG B 162 40.556 35.576 28.550 1.00 52.70 B O ATOM 2780 N ASP B 163 42.565 35.898 27.626 1.00 51.35 B N ATOM 2781 CA ASP B 163 42.243 37.200 27.071 1.00 53.37 B C ATOM 2782 CB ASP B 163 43.534 37.922 26.629 1.00 58.34 B C ATOM 2783 CG ASP B 163 43.306 39.389 26.244 1.00 67.51 B C ATOM 2784 OD1 ASP B 163 42.497 40.077 26.902 1.00 70.67 B O ATOM 2785 OD2 ASP B 163 43.960 39.866 25.289 1.00 66.93 B O ATOM 2786 C ASP B 163 41.300 36.949 25.892 1.00 50.04 B C ATOM 2787 O ASP B 163 41.725 36.868 24.743 1.00 48.16 B O ATOM 2788 N ALA B 164 40.017 36.787 26.195 1.00 45.53 B N ATOM 2789 CA ALA B 164 38.984 36.624 25.169 1.00 42.59 B C ATOM 2790 CB ALA B 164 38.929 35.171 24.690 1.00 37.81 B C ATOM 2791 C ALA B 164 37.621 37.064 25.724 1.00 37.38 B C ATOM 2792 O ALA B 164 37.386 36.972 26.930 1.00 43.20 B O ATOM 2793 N ASP B 165 36.732 37.538 24.856 1.00 33.30 B N ATOM 2794 CA ASP B 165 35.390 37.973 25.286 1.00 38.79 B C ATOM 2795 CB ASP B 165 34.654 38.653 24.149 1.00 30.05 B C ATOM 2796 CG ASP B 165 35.290 39.954 23.739 1.00 31.15 B C ATOM 2797 OD1 ASP B 165 35.786 40.676 24.626 1.00 39.03 B O ATOM 2798 OD2 ASP B 165 35.261 40.259 22.526 1.00 31.72 B O ATOM 2799 C ASP B 165 34.520 36.818 25.771 1.00 36.71 B C ATOM 2800 O ASP B 165 33.952 36.874 26.853 1.00 40.46 B O ATOM 2801 N ILE B 166 34.399 35.793 24.936 1.00 33.51 B N ATOM 2802 CA ILE B 166 33.629 34.603 25.244 1.00 36.10 B C ATOM 2803 CB ILE B 166 32.727 34.239 24.066 1.00 36.93 B C ATOM 2804 CG2 ILE B 166 32.037 32.897 24.317 1.00 37.36 B C ATOM 2805 CG1 ILE B 166 31.760 35.393 23.767 1.00 31.10 B C ATOM 2806 CD1 ILE B 166 30.897 35.199 22.510 1.00 31.74 B C ATOM 2807 C ILE B 166 34.534 33.399 25.477 1.00 37.88 B C ATOM 2808 O ILE B 166 35.193 32.932 24.554 1.00 39.73 B O ATOM 2809 N VAL B 167 34.553 32.901 26.711 1.00 35.51 B N ATOM 2810 CA VAL B 167 35.275 31.687 27.044 1.00 34.20 B C ATOM 2811 CB VAL B 167 35.854 31.753 28.450 1.00 33.45 B C ATOM 2812 CG1 VAL B 167 36.393 30.391 28.856 1.00 38.45 B C ATOM 2813 CG2 VAL B 167 36.946 32.782 28.503 1.00 37.14 B C ATOM 2814 C VAL B 167 34.340 30.490 26.993 1.00 38.39 B C ATOM 2815 O VAL B 167 33.381 30.416 27.767 1.00 41.11 B O ATOM 2816 N ILE B 168 34.611 29.565 26.081 1.00 33.64 B N ATOM 2817 CA ILE B 168 33.850 28.328 25.966 1.00 32.63 B C ATOM 2818 CB ILE B 168 33.837 27.878 24.534 1.00 33.03 B C ATOM 2819 CG2 ILE B 168 33.331 26.458 24.408 1.00 36.57 B C ATOM 2820 CG1 ILE B 168 32.967 28.824 23.731 1.00 32.62 B C ATOM 2821 CD1 ILE B 168 33.118 28.660 22.256 1.00 35.92 B C ATOM 2822 C ILE B 168 34.433 27.224 26.853 1.00 40.68 B C ATOM 2823 O ILE B 168 35.648 27.108 26.977 1.00 42.84 B O ATOM 2824 N GLN B 169 33.571 26.418 27.469 1.00 33.87 B N ATOM 2825 CA GLN B 169 34.005 25.461 28.486 1.00 31.82 B C ATOM 2826 CB GLN B 169 34.164 26.179 29.829 1.00 37.77 B C ATOM 2827 CG GLN B 169 34.136 25.288 31.051 1.00 37.07 B C ATOM 2828 CD GLN B 169 34.544 26.018 32.329 1.00 46.28 B C ATOM 2829 OE1 GLN B 169 34.969 27.179 32.304 1.00 51.90 B O ATOM 2830 NE2 GLN B 169 34.425 25.330 33.454 1.00 51.39 B N ATOM 2831 C GLN B 169 33.071 24.248 28.623 1.00 39.40 B C ATOM 2832 O GLN B 169 31.838 24.386 28.597 1.00 38.98 B O ATOM 2833 N PHE B 170 33.656 23.062 28.741 1.00 32.22 B N ATOM 2834 CA PHE B 170 32.894 21.844 28.962 1.00 33.84 B C ATOM 2835 CB PHE B 170 33.427 20.682 28.136 1.00 38.39 B C ATOM 2836 CG PHE B 170 33.008 20.684 26.689 1.00 39.53 B C ATOM 2837 CD1 PHE B 170 33.814 21.262 25.719 1.00 35.87 B C ATOM 2838 CD2 PHE B 170 31.837 20.060 26.291 1.00 37.03 B C ATOM 2839 CE1 PHE B 170 33.457 21.233 24.386 1.00 34.34 B C ATOM 2840 CE2 PHE B 170 31.472 20.033 24.958 1.00 36.58 B C ATOM 2841 CZ PHE B 170 32.290 20.622 24.001 1.00 38.24 B C ATOM 2842 C PHE B 170 33.098 21.507 30.415 1.00 38.06 B C ATOM 2843 O PHE B 170 34.212 21.621 30.922 1.00 35.38 B O ATOM 2844 N GLY B 171 32.035 21.094 31.098 1.00 36.47 B N ATOM 2845 CA GLY B 171 32.110 20.867 32.535 1.00 36.82 B C ATOM 2846 C GLY B 171 30.980 19.977 33.039 1.00 40.48 B C ATOM 2847 O GLY B 171 30.031 19.694 32.290 1.00 37.14 B O ATOM 2848 N VAL B 172 31.076 19.528 34.291 1.00 36.07 B N ATOM 2849 CA VAL B 172 30.040 18.660 34.868 1.00 38.81 B C ATOM 2850 CB VAL B 172 30.392 17.151 34.767 1.00 39.31 B C ATOM 2851 CG1 VAL B 172 30.119 16.631 33.387 1.00 40.55 B C ATOM 2852 CG2 VAL B 172 31.826 16.903 35.167 1.00 39.57 B C ATOM 2853 C VAL B 172 29.751 19.006 36.324 1.00 43.55 B C ATOM 2854 O VAL B 172 30.633 19.481 37.051 1.00 41.87 B O ATOM 2855 N ALA B 173 28.514 18.767 36.748 1.00 43.08 B N ATOM 2856 CA ALA B 173 28.101 19.134 38.091 1.00 41.48 B C ATOM 2857 CB ALA B 173 28.686 18.175 39.087 1.00 50.34 B C ATOM 2858 C ALA B 173 28.569 20.553 38.385 1.00 45.54 B C ATOM 2859 O ALA B 173 28.352 21.454 37.590 1.00 50.50 B O ATOM 2860 N GLU B 174 29.215 20.765 39.523 1.00 48.20 B N ATOM 2861 CA GLU B 174 29.789 22.076 39.788 1.00 50.01 B C ATOM 2862 CB GLU B 174 30.018 22.328 41.278 1.00 50.93 B C ATOM 2863 CG GLU B 174 30.380 23.774 41.575 1.00 52.28 B C ATOM 2864 CD GLU B 174 29.307 24.755 41.106 1.00 56.72 B C ATOM 2865 OE1 GLU B 174 28.743 25.455 41.975 1.00 56.03 B O ATOM 2866 OE2 GLU B 174 29.018 24.821 39.881 1.00 57.63 B O ATOM 2867 C GLU B 174 31.092 22.209 39.017 1.00 52.56 B C ATOM 2868 O GLU B 174 32.022 21.412 39.178 1.00 48.11 B O ATOM 2869 N HIS B 175 31.128 23.214 38.155 1.00 54.27 B N ATOM 2870 CA HIS B 175 32.256 23.429 37.280 1.00 45.01 B C ATOM 2871 CB HIS B 175 31.837 23.255 35.822 1.00 42.39 B C ATOM 2872 CG HIS B 175 30.551 23.938 35.468 1.00 42.79 B C ATOM 2873 CD2 HIS B 175 30.304 25.053 34.740 1.00 38.83 B C ATOM 2874 ND1 HIS B 175 29.320 23.455 35.853 1.00 43.53 B N ATOM 2875 CE1 HIS B 175 28.370 24.241 35.377 1.00 41.82 B C ATOM 2876 NE2 HIS B 175 28.942 25.220 34.700 1.00 37.89 B N ATOM 2877 C HIS B 175 32.845 24.801 37.523 1.00 48.59 B C ATOM 2878 O HIS B 175 33.521 25.352 36.661 1.00 49.15 B O ATOM 2879 N GLY B 176 32.577 25.357 38.702 1.00 51.45 B N ATOM 2880 CA GLY B 176 33.286 26.542 39.155 1.00 49.63 B C ATOM 2881 C GLY B 176 32.624 27.886 38.940 1.00 50.18 B C ATOM 2882 O GLY B 176 33.298 28.919 39.029 1.00 51.50 B O ATOM 2883 N ASP B 177 31.320 27.887 38.653 1.00 52.35 B N ATOM 2884 CA ASP B 177 30.550 29.139 38.585 1.00 47.14 B C ATOM 2885 CB ASP B 177 30.149 29.496 37.151 1.00 43.40 B C ATOM 2886 CG ASP B 177 29.155 28.522 36.553 1.00 43.27 B C ATOM 2887 OD1 ASP B 177 28.780 27.540 37.238 1.00 40.59 B O ATOM 2888 OD2 ASP B 177 28.773 28.746 35.380 1.00 37.09 B O ATOM 2889 C ASP B 177 29.310 29.152 39.463 1.00 51.31 B C ATOM 2890 O ASP B 177 28.497 30.073 39.377 1.00 50.90 B O ATOM 2891 N GLY B 178 29.160 28.137 40.303 1.00 50.16 B N ATOM 2892 CA GLY B 178 28.044 28.102 41.225 1.00 50.32 B C ATOM 2893 C GLY B 178 26.692 28.045 40.540 1.00 55.05 B C ATOM 2894 O GLY B 178 25.672 28.442 41.116 1.00 56.87 B O ATOM 2895 N TYR B 179 26.683 27.571 39.300 1.00 47.19 B N ATOM 2896 CA TYR B 179 25.444 27.233 38.636 1.00 42.38 B C ATOM 2897 CB TYR B 179 25.163 28.190 37.497 1.00 44.49 B C ATOM 2898 CG TYR B 179 24.949 29.629 37.912 1.00 49.32 B C ATOM 2899 CD1 TYR B 179 26.024 30.469 38.140 1.00 52.07 B C ATOM 2900 CE1 TYR B 179 25.837 31.796 38.500 1.00 52.63 B C ATOM 2901 CD2 TYR B 179 23.672 30.159 38.033 1.00 51.27 B C ATOM 2902 CE2 TYR B 179 23.473 31.490 38.396 1.00 52.62 B C ATOM 2903 CZ TYR B 179 24.564 32.305 38.628 1.00 51.35 B C ATOM 2904 OH TYR B 179 24.395 33.631 38.985 1.00 52.11 B O ATOM 2905 C TYR B 179 25.586 25.820 38.113 1.00 44.27 B C ATOM 2906 O TYR B 179 25.620 25.591 36.914 1.00 44.14 B O ATOM 2907 N PRO B 180 25.671 24.860 39.030 1.00 48.54 B N ATOM 2908 CD PRO B 180 25.399 25.091 40.462 1.00 45.44 B C ATOM 2909 CA PRO B 180 25.988 23.461 38.729 1.00 46.01 B C ATOM 2910 CB PRO B 180 25.725 22.757 40.066 1.00 48.44 B C ATOM 2911 CG PRO B 180 25.862 23.829 41.106 1.00 47.77 B C ATOM 2912 C PRO B 180 25.110 22.843 37.637 1.00 48.67 B C ATOM 2913 O PRO B 180 23.923 23.167 37.564 1.00 52.52 B O ATOM 2914 N PHE B 181 25.677 21.970 36.802 1.00 42.24 B N ATOM 2915 CA PHE B 181 24.857 21.140 35.918 1.00 42.54 B C ATOM 2916 C PHE B 181 24.301 19.944 36.689 1.00 45.49 B C ATOM 2917 CB PHE B 181 25.641 20.652 34.703 1.00 43.26 B C ATOM 2918 CG PHE B 181 26.056 21.754 33.757 1.00 45.88 B C ATOM 2919 CD1 PHE B 181 25.114 22.630 33.234 1.00 43.60 B C ATOM 2920 CD2 PHE B 181 27.391 21.901 33.380 1.00 42.30 B C ATOM 2921 CE1 PHE B 181 25.493 23.651 32.359 1.00 43.75 B C ATOM 2922 CE2 PHE B 181 27.780 22.914 32.506 1.00 40.86 B C ATOM 2923 CZ PHE B 181 26.831 23.790 31.993 1.00 42.98 B C ATOM 2924 O PHE B 181 24.555 19.796 37.884 1.00 46.37 B O ATOM 2925 N ASP B 182 23.574 19.078 35.988 1.00 46.91 B N ATOM 2926 CA ASP B 182 22.711 18.091 36.637 1.00 45.91 B C ATOM 2927 CB ASP B 182 21.260 18.581 36.575 1.00 45.38 B C ATOM 2928 CG ASP B 182 20.749 18.667 35.152 1.00 44.42 B C ATOM 2929 OD1 ASP B 182 21.598 18.820 34.265 1.00 49.75 B O ATOM 2930 OD2 ASP B 182 19.527 18.587 34.904 1.00 49.13 B O ATOM 2931 C ASP B 182 22.746 16.711 35.999 1.00 48.78 B C ATOM 2932 O ASP B 182 21.694 16.094 35.821 1.00 50.00 B O ATOM 2933 N GLY B 183 23.927 16.224 35.635 1.00 43.04 B N ATOM 2934 CA GLY B 183 24.036 14.888 35.071 1.00 43.30 B C ATOM 2935 C GLY B 183 23.263 14.737 33.778 1.00 42.37 B C ATOM 2936 O GLY B 183 22.953 15.731 33.139 1.00 41.54 B O ATOM 2937 N LYS B 184 22.932 13.504 33.399 1.00 41.17 B N ATOM 2938 CA LYS B 184 22.303 13.259 32.098 1.00 42.93 B C ATOM 2939 CB LYS B 184 22.133 11.753 31.817 1.00 41.28 B C ATOM 2940 CG LYS B 184 21.253 11.453 30.586 1.00 51.91 B C ATOM 2941 CD LYS B 184 21.660 10.175 29.813 1.00 53.07 B C ATOM 2942 CE LYS B 184 21.712 8.940 30.709 1.00 54.49 B C ATOM 2943 NZ LYS B 184 22.066 7.685 29.958 1.00 55.79 B N ATOM 2944 C LYS B 184 20.975 13.987 31.935 1.00 45.56 B C ATOM 2945 O LYS B 184 20.243 14.176 32.903 1.00 47.59 B O ATOM 2946 N ASP B 185 20.681 14.395 30.704 1.00 41.73 B N ATOM 2947 CA ASP B 185 19.447 15.111 30.379 1.00 44.67 B C ATOM 2948 CB ASP B 185 18.273 14.134 30.383 1.00 42.84 B C ATOM 2949 CG ASP B 185 18.481 12.999 29.406 1.00 53.23 B C ATOM 2950 OD1 ASP B 185 19.340 13.158 28.503 1.00 47.75 B O ATOM 2951 OD2 ASP B 185 17.808 11.952 29.538 1.00 53.77 B O ATOM 2952 C ASP B 185 19.175 16.335 31.268 1.00 41.45 B C ATOM 2953 O ASP B 185 20.021 16.756 32.045 1.00 42.42 B O ATOM 2954 N GLY B 186 17.990 16.914 31.144 1.00 42.46 B N ATOM 2955 CA GLY B 186 17.666 18.111 31.902 1.00 42.84 B C ATOM 2956 C GLY B 186 18.273 19.360 31.282 1.00 41.30 B C ATOM 2957 O GLY B 186 18.042 19.652 30.108 1.00 40.00 B O ATOM 2958 N LEU B 187 19.036 20.103 32.078 1.00 41.00 B N ATOM 2959 CA LEU B 187 19.799 21.233 31.574 1.00 40.83 B C ATOM 2960 CB LEU B 187 20.457 21.995 32.721 1.00 41.33 B C ATOM 2961 CG LEU B 187 19.595 22.570 33.835 1.00 47.32 B C ATOM 2962 CD1 LEU B 187 18.987 21.451 34.647 1.00 42.96 B C ATOM 2963 CD2 LEU B 187 20.452 23.475 34.723 1.00 46.90 B C ATOM 2964 C LEU B 187 20.903 20.706 30.661 1.00 41.47 B C ATOM 2965 O LEU B 187 21.597 19.771 31.010 1.00 42.18 B O ATOM 2966 N LEU B 188 21.072 21.303 29.493 1.00 34.96 B N ATOM 2967 CA LEU B 188 22.124 20.867 28.589 1.00 34.14 B C ATOM 2968 CB LEU B 188 21.597 20.849 27.174 1.00 34.39 B C ATOM 2969 CG LEU B 188 20.481 19.826 27.034 1.00 36.61 B C ATOM 2970 CD1 LEU B 188 19.993 19.749 25.590 1.00 25.87 B C ATOM 2971 CD2 LEU B 188 20.972 18.481 27.562 1.00 34.33 B C ATOM 2972 C LEU B 188 23.377 21.739 28.660 1.00 37.74 B C ATOM 2973 O LEU B 188 24.502 21.221 28.574 1.00 42.51 B O ATOM 2974 N ALA B 189 23.173 23.047 28.814 1.00 28.57 B N ATOM 2975 CA ALA B 189 24.244 24.019 28.886 1.00 34.98 B C ATOM 2976 CB ALA B 189 24.861 24.178 27.499 1.00 33.52 B C ATOM 2977 C ALA B 189 23.662 25.352 29.344 1.00 35.36 B C ATOM 2978 O ALA B 189 22.458 25.490 29.425 1.00 32.68 B O ATOM 2979 N HIS B 190 24.511 26.340 29.613 1.00 34.99 B N ATOM 2980 CA HIS B 190 24.052 27.720 29.782 1.00 35.10 B C ATOM 2981 CB HIS B 190 23.672 27.993 31.239 1.00 39.22 B C ATOM 2982 CG HIS B 190 24.739 27.639 32.224 1.00 39.62 B C ATOM 2983 CD2 HIS B 190 25.894 28.266 32.550 1.00 42.64 B C ATOM 2984 ND1 HIS B 190 24.675 26.520 33.024 1.00 44.16 B N ATOM 2985 CE1 HIS B 190 25.748 26.467 33.794 1.00 40.97 B C ATOM 2986 NE2 HIS B 190 26.504 27.512 33.521 1.00 38.34 B N ATOM 2987 C HIS B 190 25.096 28.737 29.310 1.00 37.47 B C ATOM 2988 O HIS B 190 26.249 28.390 29.111 1.00 41.54 B O ATOM 2989 N ALA B 191 24.685 29.987 29.140 1.00 33.77 B N ATOM 2990 CA ALA B 191 25.578 31.068 28.731 1.00 36.92 B C ATOM 2991 CB ALA B 191 25.452 31.331 27.240 1.00 31.78 B C ATOM 2992 C ALA B 191 25.216 32.329 29.501 1.00 42.41 B C ATOM 2993 O ALA B 191 24.136 32.408 30.077 1.00 33.21 B O ATOM 2994 N PHE B 192 26.112 33.312 29.480 1.00 33.88 B N ATOM 2995 CA PHE B 192 25.912 34.565 30.186 1.00 36.62 B C ATOM 2996 CB PHE B 192 26.979 34.708 31.256 1.00 34.58 B C ATOM 2997 CG PHE B 192 27.083 33.515 32.129 1.00 37.95 B C ATOM 2998 CD1 PHE B 192 26.493 33.507 33.392 1.00 40.25 B C ATOM 2999 CD2 PHE B 192 27.712 32.371 31.678 1.00 36.45 B C ATOM 3000 CE1 PHE B 192 26.565 32.382 34.203 1.00 42.49 B C ATOM 3001 CE2 PHE B 192 27.792 31.250 32.481 1.00 38.85 B C ATOM 3002 CZ PHE B 192 27.225 31.253 33.746 1.00 40.62 B C ATOM 3003 C PHE B 192 25.947 35.753 29.237 1.00 37.12 B C ATOM 3004 O PHE B 192 26.662 35.738 28.252 1.00 38.76 B O ATOM 3005 N PRO B 193 25.177 36.800 29.543 1.00 41.07 B N ATOM 3006 CD PRO B 193 24.538 37.049 30.839 1.00 39.75 B C ATOM 3007 CA PRO B 193 25.047 37.953 28.652 1.00 40.07 B C ATOM 3008 CB PRO B 193 24.021 38.841 29.375 1.00 40.84 B C ATOM 3009 CG PRO B 193 23.484 38.012 30.470 1.00 42.48 B C ATOM 3010 C PRO B 193 26.365 38.707 28.538 1.00 35.24 B C ATOM 3011 O PRO B 193 27.202 38.590 29.428 1.00 31.73 B O ATOM 3012 N PRO B 194 26.527 39.484 27.461 1.00 33.02 B N ATOM 3013 CD PRO B 194 25.529 39.630 26.389 1.00 32.41 B C ATOM 3014 CA PRO B 194 27.748 40.239 27.176 1.00 33.35 B C ATOM 3015 CB PRO B 194 27.321 41.182 26.037 1.00 32.05 B C ATOM 3016 CG PRO B 194 26.262 40.445 25.319 1.00 31.10 B C ATOM 3017 C PRO B 194 28.185 41.054 28.368 1.00 37.65 B C ATOM 3018 O PRO B 194 27.358 41.591 29.096 1.00 37.17 B O ATOM 3019 N GLY B 195 29.492 41.149 28.561 1.00 34.70 B N ATOM 3020 CA GLY B 195 30.031 42.008 29.593 1.00 41.16 B C ATOM 3021 C GLY B 195 31.357 41.466 30.087 1.00 42.46 B C ATOM 3022 O GLY B 195 31.996 40.650 29.424 1.00 43.29 B O ATOM 3023 N PRO B 196 31.768 41.899 31.272 1.00 42.13 B N ATOM 3024 CD PRO B 196 31.010 42.804 32.148 1.00 47.27 B C ATOM 3025 CA PRO B 196 33.068 41.538 31.834 1.00 39.61 B C ATOM 3026 CB PRO B 196 33.280 42.593 32.926 1.00 47.06 B C ATOM 3027 CG PRO B 196 32.089 43.537 32.843 1.00 47.56 B C ATOM 3028 C PRO B 196 33.049 40.165 32.487 1.00 44.19 B C ATOM 3029 O PRO B 196 31.984 39.620 32.805 1.00 45.41 B O ATOM 3030 N GLY B 197 34.241 39.619 32.689 1.00 45.98 B N ATOM 3031 CA GLY B 197 34.420 38.425 33.490 1.00 42.22 B C ATOM 3032 C GLY B 197 33.757 37.220 32.880 1.00 39.45 B C ATOM 3033 O GLY B 197 33.944 36.934 31.719 1.00 39.75 B O ATOM 3034 N ILE B 198 32.978 36.511 33.678 1.00 38.61 B N ATOM 3035 CA ILE B 198 32.254 35.355 33.194 1.00 40.78 B C ATOM 3036 CB ILE B 198 31.513 34.687 34.353 1.00 43.65 B C ATOM 3037 CG2 ILE B 198 30.187 35.421 34.639 1.00 36.35 B C ATOM 3038 CG1 ILE B 198 31.262 33.212 34.051 1.00 46.65 B C ATOM 3039 CD1 ILE B 198 30.392 32.540 35.100 1.00 37.85 B C ATOM 3040 C ILE B 198 31.223 35.763 32.136 1.00 38.67 B C ATOM 3041 O ILE B 198 30.701 34.930 31.391 1.00 36.53 B O ATOM 3042 N GLN B 199 30.913 37.050 32.079 1.00 36.92 B N ATOM 3043 CA GLN B 199 29.867 37.478 31.175 1.00 37.29 B C ATOM 3044 CB GLN B 199 29.408 38.905 31.502 1.00 39.10 B C ATOM 3045 CG GLN B 199 28.591 38.915 32.799 1.00 34.92 B C ATOM 3046 CD GLN B 199 28.220 40.301 33.318 1.00 44.31 B C ATOM 3047 OE1 GLN B 199 27.630 41.131 32.608 1.00 45.51 B O ATOM 3048 NE2 GLN B 199 28.520 40.538 34.592 1.00 42.78 B N ATOM 3049 C GLN B 199 30.302 37.278 29.733 1.00 38.45 B C ATOM 3050 O GLN B 199 31.410 37.642 29.367 1.00 39.31 B O ATOM 3051 N GLY B 200 29.430 36.670 28.934 1.00 31.44 B N ATOM 3052 CA GLY B 200 29.751 36.292 27.574 1.00 32.42 B C ATOM 3053 C GLY B 200 30.086 34.819 27.374 1.00 33.22 B C ATOM 3054 O GLY B 200 29.985 34.297 26.268 1.00 35.53 B O ATOM 3055 N ASP B 201 30.485 34.133 28.437 1.00 35.18 B N ATOM 3056 CA ASP B 201 30.908 32.740 28.306 1.00 33.99 B C ATOM 3057 CB ASP B 201 31.666 32.302 29.548 1.00 35.20 B C ATOM 3058 CG ASP B 201 32.805 33.219 29.874 1.00 38.12 B C ATOM 3059 OD1 ASP B 201 33.031 34.185 29.113 1.00 35.69 B O ATOM 3060 OD2 ASP B 201 33.468 32.976 30.901 1.00 38.63 B O ATOM 3061 C ASP B 201 29.766 31.766 28.048 1.00 37.51 B C ATOM 3062 O ASP B 201 28.589 32.091 28.265 1.00 39.30 B O ATOM 3063 N ALA B 202 30.126 30.569 27.596 1.00 34.77 B N ATOM 3064 CA ALA B 202 29.177 29.494 27.301 1.00 26.22 B C ATOM 3065 CB ALA B 202 28.957 29.382 25.824 1.00 31.45 B C ATOM 3066 C ALA B 202 29.745 28.202 27.837 1.00 38.74 B C ATOM 3067 O ALA B 202 30.921 27.899 27.630 1.00 42.37 B O ATOM 3068 N HIS B 203 28.919 27.436 28.534 1.00 33.06 B N ATOM 3069 CA HIS B 203 29.345 26.190 29.151 1.00 33.01 B C ATOM 3070 CB HIS B 203 29.311 26.342 30.681 1.00 36.46 B C ATOM 3071 CG HIS B 203 30.163 27.466 31.181 1.00 34.12 B C ATOM 3072 CD2 HIS B 203 30.691 28.533 30.537 1.00 37.81 B C ATOM 3073 ND1 HIS B 203 30.601 27.555 32.483 1.00 38.52 B N ATOM 3074 CE1 HIS B 203 31.339 28.641 32.629 1.00 33.78 B C ATOM 3075 NE2 HIS B 203 31.413 29.249 31.460 1.00 32.52 B N ATOM 3076 C HIS B 203 28.442 25.054 28.676 1.00 36.26 B C ATOM 3077 O HIS B 203 27.268 25.282 28.325 1.00 34.09 B O ATOM 3078 N PHE B 204 28.980 23.840 28.656 1.00 27.51 B N ATOM 3079 CA PHE B 204 28.246 22.704 28.131 1.00 30.16 B C ATOM 3080 CB PHE B 204 28.752 22.319 26.740 1.00 34.46 B C ATOM 3081 CG PHE B 204 28.611 23.416 25.731 1.00 34.96 B C ATOM 3082 CD1 PHE B 204 29.542 24.439 25.670 1.00 29.64 B C ATOM 3083 CD2 PHE B 204 27.534 23.442 24.861 1.00 28.33 B C ATOM 3084 CE1 PHE B 204 29.405 25.464 24.758 1.00 27.71 B C ATOM 3085 CE2 PHE B 204 27.392 24.474 23.948 1.00 28.25 B C ATOM 3086 CZ PHE B 204 28.334 25.491 23.910 1.00 24.48 B C ATOM 3087 C PHE B 204 28.400 21.545 29.094 1.00 37.56 B C ATOM 3088 O PHE B 204 29.490 21.310 29.613 1.00 40.20 B O ATOM 3089 N ASP B 205 27.307 20.822 29.329 1.00 34.11 B N ATOM 3090 CA ASP B 205 27.298 19.746 30.310 1.00 37.49 B C ATOM 3091 CB ASP B 205 25.860 19.484 30.784 1.00 39.62 B C ATOM 3092 CG ASP B 205 25.802 18.579 32.016 1.00 45.97 B C ATOM 3093 OD1 ASP B 205 26.819 17.938 32.376 1.00 40.17 B O ATOM 3094 OD2 ASP B 205 24.726 18.519 32.643 1.00 44.26 B O ATOM 3095 C ASP B 205 27.865 18.484 29.694 1.00 33.20 B C ATOM 3096 O ASP B 205 27.275 17.914 28.792 1.00 34.42 B O ATOM 3097 N ASP B 206 29.008 18.036 30.188 1.00 38.02 B N ATOM 3098 CA ASP B 206 29.715 16.950 29.515 1.00 39.83 B C ATOM 3099 CB ASP B 206 31.211 17.002 29.826 1.00 41.15 B C ATOM 3100 CG ASP B 206 32.074 16.492 28.674 1.00 40.58 B C ATOM 3101 OD1 ASP B 206 31.515 16.015 27.654 1.00 38.67 B O ATOM 3102 OD2 ASP B 206 33.319 16.572 28.807 1.00 39.98 B O ATOM 3103 C ASP B 206 29.111 15.622 29.929 1.00 43.00 B C ATOM 3104 O ASP B 206 29.428 14.570 29.370 1.00 45.91 B O ATOM 3105 N ASP B 207 28.231 15.692 30.923 1.00 46.26 B N ATOM 3106 CA ASP B 207 27.409 14.560 31.325 1.00 45.80 B C ATOM 3107 CB ASP B 207 26.651 14.882 32.616 1.00 41.52 B C ATOM 3108 CG ASP B 207 27.472 14.576 33.850 1.00 45.84 B C ATOM 3109 OD1 ASP B 207 28.160 13.528 33.841 1.00 47.58 B O ATOM 3110 OD2 ASP B 207 27.446 15.376 34.817 1.00 47.58 B O ATOM 3111 C ASP B 207 26.471 14.151 30.191 1.00 38.49 B C ATOM 3112 O ASP B 207 26.070 12.995 30.092 1.00 32.42 B O ATOM 3113 N GLU B 208 26.147 15.099 29.318 1.00 36.13 B N ATOM 3114 CA GLU B 208 25.439 14.773 28.090 1.00 36.42 B C ATOM 3115 CB GLU B 208 24.850 16.038 27.461 1.00 37.00 B C ATOM 3116 CG GLU B 208 23.924 16.800 28.371 1.00 39.43 B C ATOM 3117 CD GLU B 208 22.985 15.880 29.121 1.00 39.41 B C ATOM 3118 OE1 GLU B 208 22.556 14.830 28.587 1.00 38.21 B O ATOM 3119 OE2 GLU B 208 22.692 16.200 30.270 1.00 42.04 B O ATOM 3120 C GLU B 208 26.382 14.101 27.078 1.00 39.69 B C ATOM 3121 O GLU B 208 27.585 14.336 27.090 1.00 42.35 B O ATOM 3122 N LEU B 209 25.818 13.276 26.206 1.00 41.72 B N ATOM 3123 CA LEU B 209 26.534 12.742 25.063 1.00 44.33 B C ATOM 3124 CB LEU B 209 25.969 11.393 24.632 1.00 43.52 B C ATOM 3125 CG LEU B 209 26.387 10.963 23.221 1.00 41.71 B C ATOM 3126 CD1 LEU B 209 27.884 10.602 23.164 1.00 43.79 B C ATOM 3127 CD2 LEU B 209 25.540 9.806 22.746 1.00 45.11 B C ATOM 3128 C LEU B 209 26.425 13.713 23.897 1.00 45.40 B C ATOM 3129 O LEU B 209 25.339 13.904 23.328 1.00 46.63 B O ATOM 3130 N TRP B 210 27.559 14.310 23.540 1.00 38.00 B N ATOM 3131 CA TRP B 210 27.586 15.372 22.551 1.00 38.65 B C ATOM 3132 CB TRP B 210 28.549 16.456 23.008 1.00 36.01 B C ATOM 3133 CG TRP B 210 27.948 17.363 24.051 1.00 35.06 B C ATOM 3134 CD2 TRP B 210 26.845 18.253 23.864 1.00 33.87 B C ATOM 3135 CE2 TRP B 210 26.618 18.902 25.093 1.00 35.01 B C ATOM 3136 CE3 TRP B 210 26.026 18.566 22.773 1.00 33.99 B C ATOM 3137 CD1 TRP B 210 28.331 17.496 25.361 1.00 36.44 B C ATOM 3138 NE1 TRP B 210 27.539 18.426 25.992 1.00 34.15 B N ATOM 3139 CZ2 TRP B 210 25.607 19.842 25.257 1.00 33.41 B C ATOM 3140 CZ3 TRP B 210 25.030 19.505 22.935 1.00 32.07 B C ATOM 3141 CH2 TRP B 210 24.828 20.130 24.170 1.00 32.94 B C ATOM 3142 C TRP B 210 27.969 14.832 21.176 1.00 40.52 B C ATOM 3143 O TRP B 210 29.028 14.221 21.011 1.00 40.95 B O ATOM 3144 N SER B 211 27.087 15.033 20.202 1.00 35.72 B N ATOM 3145 CA SER B 211 27.306 14.522 18.859 1.00 41.69 B C ATOM 3146 CB SER B 211 26.590 13.180 18.671 1.00 44.90 B C ATOM 3147 OG SER B 211 25.185 13.349 18.615 1.00 49.12 B O ATOM 3148 C SER B 211 26.826 15.558 17.847 1.00 38.57 B C ATOM 3149 O SER B 211 26.815 16.749 18.147 1.00 37.98 B O ATOM 3150 N LEU B 212 26.434 15.124 16.658 1.00 38.78 B N ATOM 3151 CA LEU B 212 25.892 16.057 15.677 1.00 44.25 B C ATOM 3152 CB LEU B 212 26.713 16.070 14.389 1.00 50.61 B C ATOM 3153 CG LEU B 212 28.037 16.815 14.539 1.00 48.05 B C ATOM 3154 CD1 LEU B 212 28.470 17.403 13.193 1.00 49.93 B C ATOM 3155 CD2 LEU B 212 27.915 17.912 15.583 1.00 37.67 B C ATOM 3156 C LEU B 212 24.426 15.818 15.370 1.00 51.56 B C ATOM 3157 O LEU B 212 23.968 16.096 14.251 1.00 49.50 B O ATOM 3158 N GLY B 213 23.713 15.291 16.373 1.00 52.23 B N ATOM 3159 CA GLY B 213 22.260 15.324 16.430 1.00 49.49 B C ATOM 3160 C GLY B 213 21.511 14.283 15.625 1.00 54.16 B C ATOM 3161 O GLY B 213 20.353 13.976 15.927 1.00 51.68 B O ATOM 3162 N LYS B 389 22.164 13.759 14.593 1.00 52.27 B N ATOM 3163 CA LYS B 389 21.566 12.778 13.686 1.00 56.63 B C ATOM 3164 CB LYS B 389 22.573 12.460 12.579 1.00 60.09 B C ATOM 3165 CG LYS B 389 24.045 12.643 13.009 1.00 60.47 B C ATOM 3166 CD LYS B 389 24.464 11.640 14.083 1.00 56.80 B C ATOM 3167 CE LYS B 389 25.926 11.784 14.463 1.00 59.61 B C ATOM 3168 NZ LYS B 389 26.162 13.042 15.215 1.00 53.01 B N ATOM 3169 C LYS B 389 21.128 11.485 14.405 1.00 61.48 B C ATOM 3170 O LYS B 389 21.870 10.490 14.433 1.00 60.81 B O ATOM 3171 N GLY B 390 19.928 11.496 14.988 1.00 59.41 B N ATOM 3172 CA GLY B 390 19.482 10.386 15.821 1.00 56.46 B C ATOM 3173 C GLY B 390 20.453 10.114 16.962 1.00 56.43 B C ATOM 3174 O GLY B 390 20.263 9.205 17.775 1.00 49.80 B O ATOM 3175 N GLN B 391 21.507 10.922 17.021 1.00 57.20 B N ATOM 3176 CA GLN B 391 22.551 10.743 18.015 1.00 57.51 B C ATOM 3177 CB GLN B 391 23.921 11.060 17.414 1.00 53.13 B C ATOM 3178 CG GLN B 391 25.014 10.267 18.077 1.00 53.52 B C ATOM 3179 CD GLN B 391 24.686 8.800 18.057 1.00 55.50 B C ATOM 3180 OE1 GLN B 391 24.690 8.117 19.093 1.00 57.06 B O ATOM 3181 NE2 GLN B 391 24.364 8.299 16.864 1.00 59.92 B N ATOM 3182 C GLN B 391 22.318 11.611 19.255 1.00 58.15 B C ATOM 3183 O GLN B 391 22.374 11.115 20.387 1.00 53.47 B O ATOM 3184 N GLY B 392 22.064 12.904 19.014 1.00 57.43 B N ATOM 3185 CA GLY B 392 21.851 13.901 20.052 1.00 36.70 B C ATOM 3186 C GLY B 392 22.909 13.818 21.113 1.00 39.24 B C ATOM 3187 O GLY B 392 23.521 12.762 21.309 1.00 46.92 B O ATOM 3188 N TYR B 393 23.152 14.921 21.809 1.00 41.14 B N ATOM 3189 CA TYR B 393 22.562 16.222 21.521 1.00 39.08 B C ATOM 3190 CB TYR B 393 22.434 17.033 22.827 1.00 39.25 B C ATOM 3191 CG TYR B 393 21.457 16.434 23.838 1.00 43.00 B C ATOM 3192 CD1 TYR B 393 20.080 16.479 23.616 1.00 42.80 B C ATOM 3193 CE1 TYR B 393 19.183 15.935 24.519 1.00 39.67 B C ATOM 3194 CD2 TYR B 393 21.913 15.824 24.992 1.00 34.26 B C ATOM 3195 CE2 TYR B 393 21.028 15.266 25.897 1.00 47.67 B C ATOM 3196 CZ TYR B 393 19.657 15.329 25.655 1.00 46.74 B C ATOM 3197 OH TYR B 393 18.770 14.777 26.556 1.00 41.69 B O ATOM 3198 C TYR B 393 23.511 16.947 20.569 1.00 36.11 B C ATOM 3199 O TYR B 393 24.718 16.872 20.753 1.00 37.03 B O ATOM 3200 N SER B 394 22.992 17.644 19.567 1.00 32.97 B N ATOM 3201 CA SER B 394 23.878 18.344 18.637 1.00 35.15 B C ATOM 3202 CB SER B 394 23.152 18.813 17.387 1.00 33.71 B C ATOM 3203 OG SER B 394 23.768 20.013 16.940 1.00 34.93 B O ATOM 3204 C SER B 394 24.579 19.536 19.283 1.00 36.67 B C ATOM 3205 O SER B 394 23.963 20.575 19.554 1.00 31.67 B O ATOM 3206 N LEU B 395 25.877 19.384 19.523 1.00 33.16 B N ATOM 3207 CA LEU B 395 26.670 20.481 20.031 1.00 32.02 B C ATOM 3208 CB LEU B 395 28.143 20.076 20.135 1.00 34.49 B C ATOM 3209 CG LEU B 395 29.158 21.076 20.678 1.00 34.38 B C ATOM 3210 CD1 LEU B 395 28.951 21.360 22.150 1.00 30.69 B C ATOM 3211 CD2 LEU B 395 30.595 20.525 20.437 1.00 35.97 B C ATOM 3212 C LEU B 395 26.496 21.693 19.141 1.00 24.57 B C ATOM 3213 O LEU B 395 26.593 22.819 19.610 1.00 34.81 B O ATOM 3214 N PHE B 396 26.242 21.478 17.858 1.00 29.04 B N ATOM 3215 CA PHE B 396 26.064 22.597 16.922 1.00 31.77 B C ATOM 3216 CB PHE B 396 25.973 22.103 15.468 1.00 24.07 B C ATOM 3217 CG PHE B 396 25.634 23.206 14.478 1.00 25.77 B C ATOM 3218 CD1 PHE B 396 26.396 24.366 14.427 1.00 27.51 B C ATOM 3219 CD2 PHE B 396 24.572 23.093 13.617 1.00 22.89 B C ATOM 3220 CE1 PHE B 396 26.099 25.390 13.525 1.00 23.33 B C ATOM 3221 CE2 PHE B 396 24.271 24.112 12.715 1.00 25.89 B C ATOM 3222 CZ PHE B 396 25.036 25.258 12.667 1.00 24.21 B C ATOM 3223 C PHE B 396 24.853 23.496 17.233 1.00 29.41 B C ATOM 3224 O PHE B 396 24.990 24.714 17.403 1.00 27.93 B O ATOM 3225 N LEU B 397 23.666 22.883 17.242 1.00 36.58 B N ATOM 3226 CA LEU B 397 22.423 23.553 17.646 1.00 30.40 B C ATOM 3227 CB LEU B 397 21.272 22.562 17.655 1.00 29.23 B C ATOM 3228 CG LEU B 397 20.903 21.985 16.296 1.00 31.77 B C ATOM 3229 CD1 LEU B 397 19.727 21.029 16.413 1.00 33.74 B C ATOM 3230 CD2 LEU B 397 20.627 23.099 15.318 1.00 28.80 B C ATOM 3231 C LEU B 397 22.555 24.145 19.031 1.00 27.75 B C ATOM 3232 O LEU B 397 22.298 25.325 19.236 1.00 26.18 B O ATOM 3233 N VAL B 398 22.976 23.344 19.995 1.00 25.57 B N ATOM 3234 CA VAL B 398 23.065 23.883 21.339 1.00 25.14 B C ATOM 3235 CB VAL B 398 23.449 22.821 22.392 1.00 31.51 B C ATOM 3236 CG1 VAL B 398 23.750 23.491 23.733 1.00 27.68 B C ATOM 3237 CG2 VAL B 398 22.335 21.763 22.533 1.00 24.83 B C ATOM 3238 C VAL B 398 24.019 25.078 21.402 1.00 32.26 B C ATOM 3239 O VAL B 398 23.665 26.105 21.984 1.00 28.99 B O ATOM 3240 N ALA B 399 25.213 24.972 20.799 1.00 26.23 B N ATOM 3241 CA ALA B 399 26.165 26.093 20.883 1.00 27.75 B C ATOM 3242 CB ALA B 399 27.527 25.759 20.237 1.00 29.02 B C ATOM 3243 C ALA B 399 25.569 27.322 20.243 1.00 23.86 B C ATOM 3244 O ALA B 399 25.733 28.441 20.744 1.00 29.38 B O ATOM 3245 N ALA B 400 24.865 27.126 19.140 1.00 23.86 B N ATOM 3246 CA ALA B 400 24.244 28.252 18.453 1.00 27.86 B C ATOM 3247 CB ALA B 400 23.542 27.777 17.185 1.00 24.17 B C ATOM 3248 C ALA B 400 23.267 28.970 19.400 1.00 29.05 B C ATOM 3249 O ALA B 400 23.268 30.200 19.528 1.00 30.71 B O ATOM 3250 N HIS B 401 22.447 28.178 20.080 1.00 31.44 B N ATOM 3251 CA HIS B 401 21.517 28.697 21.076 1.00 31.79 B C ATOM 3252 CB HIS B 401 20.813 27.557 21.815 1.00 28.75 B C ATOM 3253 CG HIS B 401 19.799 28.042 22.810 1.00 34.11 B C ATOM 3254 CD2 HIS B 401 19.920 28.405 24.112 1.00 31.51 B C ATOM 3255 ND1 HIS B 401 18.478 28.251 22.477 1.00 31.07 B N ATOM 3256 CE1 HIS B 401 17.826 28.713 23.530 1.00 31.23 B C ATOM 3257 NE2 HIS B 401 18.673 28.804 24.539 1.00 28.38 B N ATOM 3258 C HIS B 401 22.240 29.532 22.103 1.00 27.22 B C ATOM 3259 O HIS B 401 21.939 30.711 22.286 1.00 28.31 B O ATOM 3260 N GLU B 402 23.175 28.898 22.788 1.00 28.63 B N ATOM 3261 CA GLU B 402 23.911 29.553 23.853 1.00 33.61 B C ATOM 3262 CB GLU B 402 24.972 28.616 24.435 1.00 30.91 B C ATOM 3263 CG GLU B 402 24.439 27.366 25.151 1.00 34.69 B C ATOM 3264 CD GLU B 402 23.326 27.652 26.174 1.00 35.87 B C ATOM 3265 OE1 GLU B 402 23.416 28.651 26.927 1.00 31.21 B O ATOM 3266 OE2 GLU B 402 22.366 26.849 26.214 1.00 32.20 B O ATOM 3267 C GLU B 402 24.586 30.829 23.370 1.00 33.75 B C ATOM 3268 O GLU B 402 24.649 31.832 24.101 1.00 33.88 B O ATOM 3269 N PHE B 403 25.112 30.787 22.150 1.00 31.20 B N ATOM 3270 CA PHE B 403 25.869 31.920 21.626 1.00 29.83 B C ATOM 3271 CB PHE B 403 26.560 31.581 20.289 1.00 30.07 B C ATOM 3272 CG PHE B 403 27.773 30.644 20.426 1.00 26.45 B C ATOM 3273 CD1 PHE B 403 28.333 30.375 21.661 1.00 26.41 B C ATOM 3274 CD2 PHE B 403 28.361 30.076 19.302 1.00 31.44 B C ATOM 3275 CE1 PHE B 403 29.441 29.516 21.791 1.00 35.79 B C ATOM 3276 CE2 PHE B 403 29.468 29.229 19.413 1.00 27.00 B C ATOM 3277 CZ PHE B 403 30.007 28.940 20.652 1.00 28.81 B C ATOM 3278 C PHE B 403 24.907 33.085 21.481 1.00 33.20 B C ATOM 3279 O PHE B 403 25.305 34.239 21.572 1.00 30.19 B O ATOM 3280 N GLY B 404 23.631 32.765 21.274 1.00 31.92 B N ATOM 3281 CA GLY B 404 22.560 33.756 21.295 1.00 28.28 B C ATOM 3282 C GLY B 404 22.577 34.563 22.580 1.00 26.84 B C ATOM 3283 O GLY B 404 22.588 35.780 22.552 1.00 26.56 B O ATOM 3284 N HIS B 405 22.628 33.876 23.707 1.00 29.62 B N ATOM 3285 CA HIS B 405 22.698 34.517 25.016 1.00 31.65 B C ATOM 3286 CB HIS B 405 22.652 33.459 26.133 1.00 30.34 B C ATOM 3287 CG HIS B 405 21.352 32.708 26.238 1.00 36.49 B C ATOM 3288 CD2 HIS B 405 21.090 31.412 26.550 1.00 32.52 B C ATOM 3289 ND1 HIS B 405 20.125 33.317 26.091 1.00 34.57 B N ATOM 3290 CE1 HIS B 405 19.165 32.429 26.291 1.00 32.79 B C ATOM 3291 NE2 HIS B 405 19.721 31.270 26.578 1.00 27.14 B N ATOM 3292 C HIS B 405 23.996 35.293 25.172 1.00 35.90 B C ATOM 3293 O HIS B 405 24.027 36.363 25.792 1.00 33.62 B O ATOM 3294 N ALA B 406 25.088 34.737 24.650 1.00 32.66 B N ATOM 3295 CA ALA B 406 26.389 35.382 24.831 1.00 31.44 B C ATOM 3296 CB ALA B 406 27.506 34.498 24.328 1.00 31.27 B C ATOM 3297 C ALA B 406 26.366 36.708 24.092 1.00 31.80 B C ATOM 3298 O ALA B 406 27.172 37.600 24.348 1.00 33.25 B O ATOM 3299 N LEU B 407 25.423 36.834 23.169 1.00 26.21 B N ATOM 3300 CA LEU B 407 25.283 38.072 22.421 1.00 27.94 B C ATOM 3301 CB LEU B 407 24.863 37.759 20.999 1.00 26.53 B C ATOM 3302 CG LEU B 407 25.988 37.110 20.198 1.00 27.30 B C ATOM 3303 CD1 LEU B 407 25.639 37.205 18.751 1.00 30.22 B C ATOM 3304 CD2 LEU B 407 27.315 37.798 20.477 1.00 29.21 B C ATOM 3305 C LEU B 407 24.290 39.049 23.054 1.00 33.13 B C ATOM 3306 O LEU B 407 24.176 40.191 22.607 1.00 31.07 B O ATOM 3307 N GLY B 408 23.581 38.582 24.086 1.00 33.28 B N ATOM 3308 CA GLY B 408 22.586 39.373 24.805 1.00 34.97 B C ATOM 3309 C GLY B 408 21.120 39.030 24.515 1.00 34.84 B C ATOM 3310 O GLY B 408 20.238 39.854 24.743 1.00 32.85 B O ATOM 3311 N LEU B 409 20.846 37.822 24.021 1.00 25.84 B N ATOM 3312 CA LEU B 409 19.476 37.460 23.675 1.00 34.40 B C ATOM 3313 CB LEU B 409 19.414 36.622 22.403 1.00 34.50 B C ATOM 3314 CG LEU B 409 19.693 37.293 21.065 1.00 29.08 B C ATOM 3315 CD1 LEU B 409 19.490 36.245 19.974 1.00 23.23 B C ATOM 3316 CD2 LEU B 409 18.788 38.500 20.841 1.00 24.33 B C ATOM 3317 C LEU B 409 18.857 36.668 24.805 1.00 35.13 B C ATOM 3318 O LEU B 409 19.558 35.967 25.530 1.00 32.49 B O ATOM 3319 N ASP B 410 17.538 36.775 24.944 1.00 38.05 B N ATOM 3320 CA ASP B 410 16.812 35.984 25.936 1.00 36.91 B C ATOM 3321 CB ASP B 410 15.870 36.877 26.732 1.00 35.50 B C ATOM 3322 CG ASP B 410 16.621 37.808 27.628 1.00 41.41 B C ATOM 3323 OD1 ASP B 410 17.375 37.265 28.455 1.00 46.89 B O ATOM 3324 OD2 ASP B 410 16.495 39.053 27.489 1.00 41.79 B O ATOM 3325 C ASP B 410 16.040 34.899 25.238 1.00 35.50 B C ATOM 3326 O ASP B 410 16.116 34.776 24.024 1.00 30.42 B O ATOM 3327 N HIS B 411 15.278 34.119 25.993 1.00 32.52 B N ATOM 3328 CA HIS B 411 14.511 33.050 25.374 1.00 31.15 B C ATOM 3329 CB HIS B 411 14.037 32.051 26.417 1.00 38.06 B C ATOM 3330 CG HIS B 411 15.098 31.088 26.829 1.00 35.86 B C ATOM 3331 CD2 HIS B 411 16.040 30.446 26.103 1.00 33.28 B C ATOM 3332 ND1 HIS B 411 15.295 30.704 28.138 1.00 35.23 B N ATOM 3333 CE1 HIS B 411 16.299 29.849 28.198 1.00 33.38 B C ATOM 3334 NE2 HIS B 411 16.764 29.674 26.975 1.00 34.56 B N ATOM 3335 C HIS B 411 13.352 33.574 24.548 1.00 32.41 B C ATOM 3336 O HIS B 411 12.838 34.662 24.778 1.00 35.20 B O ATOM 3337 N SER B 412 12.964 32.798 23.557 1.00 31.56 B N ATOM 3338 CA SER B 412 11.826 33.128 22.733 1.00 31.59 B C ATOM 3339 CB SER B 412 12.217 32.963 21.264 1.00 26.45 B C ATOM 3340 OG SER B 412 11.120 32.684 20.419 1.00 22.22 B O ATOM 3341 C SER B 412 10.630 32.229 23.105 1.00 32.63 B C ATOM 3342 O SER B 412 10.792 31.113 23.612 1.00 35.31 B O ATOM 3343 N SER B 413 9.430 32.708 22.823 1.00 31.37 B N ATOM 3344 CA SER B 413 8.251 31.890 23.071 1.00 38.71 B C ATOM 3345 CB SER B 413 7.137 32.710 23.710 1.00 34.94 B C ATOM 3346 OG SER B 413 6.641 33.658 22.798 1.00 45.15 B O ATOM 3347 C SER B 413 7.765 31.229 21.802 1.00 42.59 B C ATOM 3348 O SER B 413 6.761 30.515 21.830 1.00 43.20 B O ATOM 3349 N VAL B 414 8.471 31.445 20.685 1.00 38.36 B N ATOM 3350 CA VAL B 414 8.154 30.701 19.457 1.00 34.96 B C ATOM 3351 CB VAL B 414 8.552 31.430 18.168 1.00 33.22 B C ATOM 3352 CG1 VAL B 414 8.069 30.631 16.963 1.00 32.38 B C ATOM 3353 CG2 VAL B 414 7.972 32.819 18.133 1.00 26.89 B C ATOM 3354 C VAL B 414 8.810 29.333 19.455 1.00 37.88 B C ATOM 3355 O VAL B 414 10.032 29.215 19.408 1.00 36.44 B O ATOM 3356 N PRO B 415 7.990 28.287 19.495 1.00 38.18 B N ATOM 3357 CD PRO B 415 6.537 28.316 19.262 1.00 41.23 B C ATOM 3358 CA PRO B 415 8.496 26.937 19.727 1.00 41.04 B C ATOM 3359 CB PRO B 415 7.255 26.055 19.542 1.00 37.81 B C ATOM 3360 CG PRO B 415 6.099 26.982 19.750 1.00 41.90 B C ATOM 3361 C PRO B 415 9.556 26.564 18.710 1.00 39.22 B C ATOM 3362 O PRO B 415 10.471 25.825 19.049 1.00 40.11 B O ATOM 3363 N GLU B 416 9.441 27.054 17.485 1.00 36.64 B N ATOM 3364 CA GLU B 416 10.411 26.645 16.473 1.00 44.82 B C ATOM 3365 CB GLU B 416 9.736 26.280 15.137 1.00 45.54 B C ATOM 3366 CG GLU B 416 8.642 27.245 14.668 1.00 56.24 B C ATOM 3367 CD GLU B 416 7.343 27.115 15.454 1.00 47.39 B C ATOM 3368 OE1 GLU B 416 6.947 25.975 15.782 1.00 50.92 B O ATOM 3369 OE2 GLU B 416 6.721 28.160 15.732 1.00 48.08 B O ATOM 3370 C GLU B 416 11.594 27.618 16.290 1.00 43.63 B C ATOM 3371 O GLU B 416 12.440 27.404 15.421 1.00 40.00 B O ATOM 3372 N ALA B 417 11.662 28.659 17.121 1.00 37.37 B N ATOM 3373 CA ALA B 417 12.782 29.595 17.077 1.00 35.20 B C ATOM 3374 CB ALA B 417 12.429 30.904 17.753 1.00 30.24 B C ATOM 3375 C ALA B 417 14.021 28.994 17.721 1.00 34.09 B C ATOM 3376 O ALA B 417 13.929 28.217 18.669 1.00 31.19 B O ATOM 3377 N LEU B 418 15.191 29.370 17.208 1.00 34.15 B N ATOM 3378 CA LEU B 418 16.447 28.911 17.805 1.00 33.75 B C ATOM 3379 CB LEU B 418 17.636 29.556 17.079 1.00 29.86 B C ATOM 3380 CG LEU B 418 18.987 29.289 17.732 1.00 27.52 B C ATOM 3381 CD1 LEU B 418 19.249 27.796 17.765 1.00 27.43 B C ATOM 3382 CD2 LEU B 418 20.121 30.042 16.998 1.00 27.87 B C ATOM 3383 C LEU B 418 16.525 29.233 19.305 1.00 26.38 B C ATOM 3384 O LEU B 418 17.068 28.454 20.115 1.00 23.36 B O ATOM 3385 N MET B 419 16.022 30.404 19.674 1.00 28.01 B N ATOM 3386 CA MET B 419 16.149 30.840 21.060 1.00 27.85 B C ATOM 3387 CB MET B 419 16.239 32.359 21.178 1.00 26.67 B C ATOM 3388 CG MET B 419 17.565 32.969 20.639 1.00 28.74 B C ATOM 3389 SD MET B 419 19.079 32.027 21.011 1.00 25.96 B S ATOM 3390 CE MET B 419 19.342 32.299 22.738 1.00 24.53 B C ATOM 3391 C MET B 419 15.053 30.245 21.998 1.00 31.91 B C ATOM 3392 O MET B 419 15.073 30.488 23.195 1.00 36.09 B O ATOM 3393 N TYR B 420 14.143 29.437 21.461 1.00 30.26 B N ATOM 3394 CA TYR B 420 13.263 28.613 22.315 1.00 30.76 B C ATOM 3395 CB TYR B 420 12.407 27.707 21.449 1.00 33.96 B C ATOM 3396 CG TYR B 420 11.161 27.135 22.119 1.00 44.14 B C ATOM 3397 CD1 TYR B 420 10.048 27.939 22.397 1.00 38.43 B C ATOM 3398 CE1 TYR B 420 8.902 27.401 22.996 1.00 41.12 B C ATOM 3399 CD2 TYR B 420 11.093 25.786 22.447 1.00 39.78 B C ATOM 3400 CE2 TYR B 420 9.951 25.241 23.040 1.00 39.43 B C ATOM 3401 CZ TYR B 420 8.867 26.049 23.308 1.00 43.36 B C ATOM 3402 OH TYR B 420 7.761 25.487 23.907 1.00 46.01 B O ATOM 3403 C TYR B 420 14.122 27.762 23.219 1.00 33.37 B C ATOM 3404 O TYR B 420 15.105 27.182 22.765 1.00 34.51 B O ATOM 3405 N PRO B 421 13.756 27.668 24.508 1.00 34.99 B N ATOM 3406 CD PRO B 421 12.463 28.132 25.048 1.00 38.45 B C ATOM 3407 CA PRO B 421 14.595 27.046 25.542 1.00 33.82 B C ATOM 3408 CB PRO B 421 13.849 27.367 26.851 1.00 39.33 B C ATOM 3409 CG PRO B 421 12.759 28.354 26.480 1.00 39.11 B C ATOM 3410 C PRO B 421 14.755 25.536 25.440 1.00 32.34 B C ATOM 3411 O PRO B 421 15.707 24.996 26.024 1.00 32.23 B O ATOM 3412 N MET B 422 13.835 24.867 24.755 1.00 34.19 B N ATOM 3413 CA MET B 422 13.806 23.413 24.752 1.00 34.43 B C ATOM 3414 CB MET B 422 12.381 22.910 24.572 1.00 38.61 B C ATOM 3415 CG MET B 422 11.456 22.986 25.777 1.00 42.46 B C ATOM 3416 SD MET B 422 9.965 22.018 25.380 1.00 45.95 B S ATOM 3417 CE MET B 422 8.697 23.251 25.705 1.00 41.72 B C ATOM 3418 C MET B 422 14.594 22.881 23.585 1.00 36.25 B C ATOM 3419 O MET B 422 14.440 23.358 22.459 1.00 36.62 B O ATOM 3420 N TYR B 423 15.397 21.856 23.841 1.00 40.39 B N ATOM 3421 CA TYR B 423 16.185 21.237 22.786 1.00 35.65 B C ATOM 3422 CB TYR B 423 17.085 20.144 23.323 1.00 40.41 B C ATOM 3423 CG TYR B 423 17.856 19.485 22.211 1.00 43.35 B C ATOM 3424 CD1 TYR B 423 17.482 18.245 21.722 1.00 37.50 B C ATOM 3425 CE1 TYR B 423 18.179 17.649 20.697 1.00 37.38 B C ATOM 3426 CD2 TYR B 423 18.943 20.130 21.615 1.00 39.34 B C ATOM 3427 CE2 TYR B 423 19.651 19.534 20.587 1.00 38.36 B C ATOM 3428 CZ TYR B 423 19.263 18.299 20.126 1.00 39.14 B C ATOM 3429 OH TYR B 423 19.964 17.701 19.106 1.00 32.27 B O ATOM 3430 C TYR B 423 15.288 20.621 21.760 1.00 40.86 B C ATOM 3431 O TYR B 423 14.314 19.941 22.100 1.00 44.88 B O ATOM 3432 N ARG B 424 15.621 20.845 20.501 1.00 37.73 B N ATOM 3433 CA ARG B 424 14.796 20.380 19.415 1.00 41.11 B C ATOM 3434 CB ARG B 424 13.683 21.392 19.122 1.00 41.89 B C ATOM 3435 CG ARG B 424 12.771 20.938 17.998 1.00 43.79 B C ATOM 3436 CD ARG B 424 11.867 22.039 17.491 1.00 53.41 B C ATOM 3437 NE ARG B 424 12.597 23.173 16.921 1.00 55.24 B N ATOM 3438 CZ ARG B 424 12.866 23.319 15.626 1.00 54.90 B C ATOM 3439 NH1 ARG B 424 12.478 22.383 14.759 1.00 55.37 B N ATOM 3440 NH2 ARG B 424 13.521 24.401 15.198 1.00 47.69 B N ATOM 3441 C ARG B 424 15.638 20.199 18.166 1.00 41.08 B C ATOM 3442 O ARG B 424 16.002 21.172 17.519 1.00 39.68 B O ATOM 3443 N PHE B 425 15.916 18.952 17.818 1.00 41.93 B N ATOM 3444 CA PHE B 425 16.744 18.648 16.659 1.00 37.65 B C ATOM 3445 CB PHE B 425 17.153 17.178 16.694 1.00 42.16 B C ATOM 3446 CG PHE B 425 17.997 16.770 15.542 1.00 39.36 B C ATOM 3447 CD1 PHE B 425 19.376 16.926 15.587 1.00 44.56 B C ATOM 3448 CD2 PHE B 425 17.418 16.250 14.402 1.00 40.07 B C ATOM 3449 CE1 PHE B 425 20.163 16.570 14.504 1.00 46.39 B C ATOM 3450 CE2 PHE B 425 18.199 15.888 13.319 1.00 48.81 B C ATOM 3451 CZ PHE B 425 19.575 16.047 13.375 1.00 47.79 B C ATOM 3452 C PHE B 425 16.067 18.993 15.326 1.00 37.74 B C ATOM 3453 O PHE B 425 14.929 18.601 15.069 1.00 42.44 B O ATOM 3454 N THR B 426 16.774 19.743 14.487 1.00 41.03 B N ATOM 3455 CA THR B 426 16.342 20.005 13.110 1.00 42.02 B C ATOM 3456 CB THR B 426 15.735 21.430 12.944 1.00 40.51 B C ATOM 3457 OG1 THR B 426 15.104 21.553 11.656 1.00 35.09 B O ATOM 3458 CG2 THR B 426 16.802 22.509 13.088 1.00 35.93 B C ATOM 3459 C THR B 426 17.508 19.832 12.129 1.00 43.76 B C ATOM 3460 O THR B 426 18.678 19.899 12.517 1.00 37.99 B O ATOM 3461 N GLU B 427 17.175 19.594 10.864 1.00 47.40 B N ATOM 3462 CA GLU B 427 18.155 19.540 9.785 1.00 45.24 B C ATOM 3463 CB GLU B 427 17.763 18.469 8.770 1.00 50.25 B C ATOM 3464 CG GLU B 427 17.391 17.124 9.365 1.00 58.90 B C ATOM 3465 CD GLU B 427 18.469 16.068 9.184 1.00 56.72 B C ATOM 3466 OE1 GLU B 427 19.539 16.171 9.825 1.00 61.62 B O ATOM 3467 OE2 GLU B 427 18.235 15.123 8.403 1.00 55.13 B O ATOM 3468 C GLU B 427 18.184 20.886 9.062 1.00 46.83 B C ATOM 3469 O GLU B 427 19.130 21.187 8.299 1.00 42.48 B O ATOM 3470 N GLY B 428 17.130 21.674 9.282 1.00 31.53 B N ATOM 3471 CA GLY B 428 16.942 22.930 8.581 1.00 31.53 B C ATOM 3472 C GLY B 428 17.801 24.062 9.110 1.00 28.85 B C ATOM 3473 O GLY B 428 18.440 23.931 10.163 1.00 30.01 B O ATOM 3474 N PRO B 429 17.809 25.192 8.391 1.00 23.94 B N ATOM 3475 CD PRO B 429 16.997 25.457 7.203 1.00 22.51 B C ATOM 3476 CA PRO B 429 18.495 26.391 8.874 1.00 25.81 B C ATOM 3477 CB PRO B 429 18.016 27.483 7.912 1.00 22.99 B C ATOM 3478 CG PRO B 429 17.578 26.710 6.694 1.00 26.40 B C ATOM 3479 C PRO B 429 17.976 26.683 10.270 1.00 25.78 B C ATOM 3480 O PRO B 429 16.767 26.840 10.457 1.00 31.58 B O ATOM 3481 N PRO B 430 18.878 26.758 11.236 1.00 27.15 B N ATOM 3482 CD PRO B 430 20.336 26.636 11.045 1.00 24.41 B C ATOM 3483 CA PRO B 430 18.516 27.006 12.636 1.00 29.50 B C ATOM 3484 CB PRO B 430 19.867 26.909 13.365 1.00 33.21 B C ATOM 3485 CG PRO B 430 20.799 26.159 12.366 1.00 25.62 B C ATOM 3486 C PRO B 430 17.848 28.370 12.896 1.00 36.36 B C ATOM 3487 O PRO B 430 16.947 28.413 13.728 1.00 35.88 B O ATOM 3488 N LEU B 431 18.261 29.457 12.243 1.00 26.72 B N ATOM 3489 CA LEU B 431 17.698 30.759 12.598 1.00 29.21 B C ATOM 3490 CB LEU B 431 18.506 31.909 11.991 1.00 31.16 B C ATOM 3491 CG LEU B 431 19.935 32.097 12.489 1.00 35.04 B C ATOM 3492 CD1 LEU B 431 20.520 33.336 11.872 1.00 23.70 B C ATOM 3493 CD2 LEU B 431 19.970 32.183 14.006 1.00 27.87 B C ATOM 3494 C LEU B 431 16.265 30.896 12.111 1.00 30.49 B C ATOM 3495 O LEU B 431 15.949 30.488 10.990 1.00 27.06 B O ATOM 3496 N HIS B 432 15.412 31.504 12.934 1.00 31.54 B N ATOM 3497 CA HIS B 432 14.067 31.887 12.493 1.00 27.52 B C ATOM 3498 CB HIS B 432 13.021 31.125 13.309 1.00 31.55 B C ATOM 3499 CG HIS B 432 12.848 29.699 12.881 1.00 28.77 B C ATOM 3500 CD2 HIS B 432 11.915 29.112 12.096 1.00 30.65 B C ATOM 3501 ND1 HIS B 432 13.717 28.697 13.261 1.00 29.33 B N ATOM 3502 CE1 HIS B 432 13.319 27.551 12.734 1.00 33.00 B C ATOM 3503 NE2 HIS B 432 12.229 27.775 12.022 1.00 27.70 B N ATOM 3504 C HIS B 432 13.831 33.405 12.580 1.00 23.89 B C ATOM 3505 O HIS B 432 14.578 34.121 13.247 1.00 24.79 B O ATOM 3506 N LYS B 433 12.777 33.885 11.929 1.00 25.84 B N ATOM 3507 CA LYS B 433 12.457 35.315 11.938 1.00 27.89 B C ATOM 3508 CB LYS B 433 11.037 35.558 11.422 1.00 26.05 B C ATOM 3509 CG LYS B 433 10.819 35.221 9.955 1.00 34.94 B C ATOM 3510 CD LYS B 433 9.353 35.319 9.559 1.00 35.41 B C ATOM 3511 CE LYS B 433 9.151 35.007 8.087 1.00 35.38 B C ATOM 3512 NZ LYS B 433 9.425 36.203 7.247 1.00 34.82 B N ATOM 3513 C LYS B 433 12.571 35.905 13.327 1.00 27.17 B C ATOM 3514 O LYS B 433 13.058 37.028 13.502 1.00 29.29 B O ATOM 3515 N ASP B 434 12.145 35.143 14.330 1.00 25.80 B N ATOM 3516 CA ASP B 434 12.099 35.683 15.701 1.00 30.13 B C ATOM 3517 CB ASP B 434 11.186 34.867 16.662 1.00 23.63 B C ATOM 3518 CG ASP B 434 10.951 35.604 17.975 1.00 22.61 B C ATOM 3519 OD1 ASP B 434 10.276 36.676 17.960 1.00 25.59 B O ATOM 3520 OD2 ASP B 434 11.499 35.164 18.999 1.00 23.53 B O ATOM 3521 C ASP B 434 13.480 35.877 16.306 1.00 26.91 B C ATOM 3522 O ASP B 434 13.722 36.834 17.039 1.00 28.29 B O ATOM 3523 N ASP B 435 14.374 34.948 16.013 1.00 28.16 B N ATOM 3524 CA ASP B 435 15.783 35.115 16.332 1.00 30.27 B C ATOM 3525 CB ASP B 435 16.529 33.855 15.928 1.00 31.09 B C ATOM 3526 CG ASP B 435 15.925 32.607 16.536 1.00 30.39 B C ATOM 3527 OD1 ASP B 435 15.911 32.491 17.789 1.00 29.43 B O ATOM 3528 OD2 ASP B 435 15.492 31.738 15.758 1.00 28.40 B O ATOM 3529 C ASP B 435 16.413 36.335 15.635 1.00 19.99 B C ATOM 3530 O ASP B 435 17.167 37.084 16.245 1.00 27.70 B O ATOM 3531 N VAL B 436 16.099 36.546 14.373 1.00 24.03 B N ATOM 3532 CA VAL B 436 16.714 37.665 13.644 1.00 27.92 B C ATOM 3533 CB VAL B 436 16.443 37.579 12.118 1.00 27.14 B C ATOM 3534 CG1 VAL B 436 17.001 38.786 11.392 1.00 27.02 B C ATOM 3535 CG2 VAL B 436 17.043 36.297 11.546 1.00 28.95 B C ATOM 3536 C VAL B 436 16.234 38.997 14.209 1.00 31.84 B C ATOM 3537 O VAL B 436 17.033 39.897 14.521 1.00 27.16 B O ATOM 3538 N ASN B 437 14.916 39.115 14.361 1.00 31.95 B N ATOM 3539 CA ASN B 437 14.333 40.309 14.974 1.00 28.82 B C ATOM 3540 CB ASN B 437 12.823 40.133 15.158 1.00 32.65 B C ATOM 3541 CG ASN B 437 12.094 40.041 13.844 1.00 34.13 B C ATOM 3542 OD1 ASN B 437 12.465 40.688 12.858 1.00 35.07 B O ATOM 3543 ND2 ASN B 437 11.034 39.248 13.821 1.00 38.57 B N ATOM 3544 C ASN B 437 14.977 40.605 16.298 1.00 19.64 B C ATOM 3545 O ASN B 437 15.404 41.715 16.551 1.00 27.86 B O ATOM 3546 N GLY B 438 15.051 39.605 17.151 1.00 19.87 B N ATOM 3547 CA GLY B 438 15.685 39.802 18.442 1.00 22.69 B C ATOM 3548 C GLY B 438 17.097 40.337 18.260 1.00 28.94 B C ATOM 3549 O GLY B 438 17.526 41.302 18.903 1.00 25.63 B O ATOM 3550 N ILE B 439 17.842 39.736 17.346 1.00 31.08 B N ATOM 3551 CA ILE B 439 19.247 40.143 17.249 1.00 28.32 B C ATOM 3552 CB ILE B 439 20.108 39.117 16.489 1.00 26.70 B C ATOM 3553 CG2 ILE B 439 19.835 39.185 14.990 1.00 23.81 B C ATOM 3554 CG1 ILE B 439 21.577 39.275 16.900 1.00 24.32 B C ATOM 3555 CD1 ILE B 439 21.792 39.033 18.376 1.00 25.13 B C ATOM 3556 C ILE B 439 19.332 41.539 16.658 1.00 23.79 B C ATOM 3557 O ILE B 439 20.128 42.356 17.100 1.00 30.30 B O ATOM 3558 N ARG B 440 18.476 41.843 15.698 1.00 26.32 B N ATOM 3559 CA ARG B 440 18.511 43.177 15.130 1.00 26.31 B C ATOM 3560 CB ARG B 440 17.645 43.276 13.890 1.00 28.74 B C ATOM 3561 CG ARG B 440 18.211 42.518 12.722 1.00 28.48 B C ATOM 3562 CD ARG B 440 17.453 42.780 11.465 1.00 35.18 B C ATOM 3563 NE ARG B 440 17.744 41.768 10.460 1.00 34.95 B N ATOM 3564 CZ ARG B 440 17.278 41.788 9.215 1.00 36.37 B C ATOM 3565 NH1 ARG B 440 16.502 42.784 8.791 1.00 33.80 B N ATOM 3566 NH2 ARG B 440 17.609 40.813 8.382 1.00 33.22 B N ATOM 3567 C ARG B 440 18.105 44.227 16.145 1.00 33.33 B C ATOM 3568 O ARG B 440 18.507 45.382 16.039 1.00 32.00 B O ATOM 3569 N HIS B 441 17.307 43.840 17.136 1.00 33.60 B N ATOM 3570 CA HIS B 441 16.853 44.837 18.102 1.00 34.46 B C ATOM 3571 CB HIS B 441 15.657 44.342 18.921 1.00 36.90 B C ATOM 3572 CG HIS B 441 15.270 45.282 20.021 1.00 42.77 B C ATOM 3573 CD2 HIS B 441 14.648 46.487 19.987 1.00 41.09 B C ATOM 3574 ND1 HIS B 441 15.578 45.046 21.345 1.00 43.46 B N ATOM 3575 CE1 HIS B 441 15.147 46.057 22.083 1.00 45.60 B C ATOM 3576 NE2 HIS B 441 14.582 46.944 21.283 1.00 50.21 B N ATOM 3577 C HIS B 441 18.011 45.263 19.008 1.00 35.34 B C ATOM 3578 O HIS B 441 18.034 46.394 19.517 1.00 38.38 B O ATOM 3579 N LEU B 442 18.984 44.372 19.194 1.00 33.75 B N ATOM 3580 CA LEU B 442 20.206 44.726 19.934 1.00 32.13 B C ATOM 3581 CB LEU B 442 20.847 43.484 20.573 1.00 31.05 B C ATOM 3582 CG LEU B 442 20.248 43.004 21.896 1.00 35.48 B C ATOM 3583 CD1 LEU B 442 18.726 42.961 21.850 1.00 37.69 B C ATOM 3584 CD2 LEU B 442 20.790 41.655 22.276 1.00 34.25 B C ATOM 3585 C LEU B 442 21.251 45.476 19.078 1.00 34.07 B C ATOM 3586 O LEU B 442 21.749 46.527 19.484 1.00 38.06 B O ATOM 3587 N TYR B 443 21.569 44.941 17.898 1.00 32.79 B N ATOM 3588 CA TYR B 443 22.693 45.443 17.088 1.00 34.58 B C ATOM 3589 CB TYR B 443 23.695 44.298 16.815 1.00 29.55 B C ATOM 3590 CG TYR B 443 24.254 43.709 18.095 1.00 27.01 B C ATOM 3591 CD1 TYR B 443 23.824 42.479 18.578 1.00 25.66 B C ATOM 3592 CE1 TYR B 443 24.318 41.970 19.756 1.00 20.51 B C ATOM 3593 CD2 TYR B 443 25.162 44.419 18.850 1.00 28.32 B C ATOM 3594 CE2 TYR B 443 25.666 43.916 20.032 1.00 29.77 B C ATOM 3595 CZ TYR B 443 25.241 42.693 20.479 1.00 27.46 B C ATOM 3596 OH TYR B 443 25.774 42.212 21.663 1.00 31.04 B O ATOM 3597 C TYR B 443 22.303 46.151 15.785 1.00 35.90 B C ATOM 3598 O TYR B 443 23.150 46.763 15.115 1.00 35.10 B O ATOM 3599 N GLY B 444 21.033 46.045 15.409 1.00 29.94 B N ATOM 3600 CA GLY B 444 20.502 46.798 14.287 1.00 23.72 B C ATOM 3601 C GLY B 444 20.229 45.972 13.058 1.00 24.22 B C ATOM 3602 O GLY B 444 19.712 46.519 12.086 1.00 33.74 B O ATOM 3603 ZN ZN B 500 18.926 29.347 26.591 1.00 32.37 B Zn ATOM 3604 ZN ZN B 501 28.572 27.259 34.032 1.00 42.34 B Zn ATOM 3605 CA CA B 502 22.431 17.803 31.961 1.00 41.66 B Ca ATOM 3606 CA CA B 504 33.866 36.697 29.276 1.00 49.72 B Ca ATOM 3607 CA CA B 505 32.637 45.904 25.506 1.00 54.30 B Ca TER 3608 CA B 505 ATOM 3609 C01 LIG C 1 20.376 35.685 28.031 1.00 46.05 A C ATOM 3610 O02 LIG C 1 20.646 37.080 28.151 1.00 52.57 A O ATOM 3611 C03 LIG C 1 20.132 37.822 29.196 1.00 50.59 A C ATOM 3612 C04 LIG C 1 19.422 39.029 29.001 1.00 51.04 A C ATOM 3613 C05 LIG C 1 18.941 39.808 30.065 1.00 53.55 A C ATOM 3614 C06 LIG C 1 19.160 39.419 31.392 1.00 57.54 A C ATOM 3615 C07 LIG C 1 19.883 38.203 31.580 1.00 54.92 A C ATOM 3616 C08 LIG C 1 20.397 37.354 30.544 1.00 47.25 A C ATOM 3617 N09 LIG C 1 21.104 36.090 30.869 1.00 48.66 A N ATOM 3618 C10 LIG C 1 21.199 35.094 31.916 1.00 51.94 A C ATOM 3619 C11 LIG C 1 20.523 35.259 33.182 1.00 42.58 A C ATOM 3620 C12 LIG C 1 20.667 34.362 34.200 1.00 46.59 A C ATOM 3621 C13 LIG C 1 21.489 33.217 34.066 1.00 46.36 A C ATOM 3622 C14 LIG C 1 21.639 32.281 35.133 1.00 46.01 A C ATOM 3623 C15 LIG C 1 22.417 31.179 34.989 1.00 52.78 A C ATOM 3624 C16 LIG C 1 23.099 30.994 33.754 1.00 48.48 A C ATOM 3625 C17 LIG C 1 22.981 31.886 32.722 1.00 44.53 A C ATOM 3626 C18 LIG C 1 22.149 33.071 32.817 1.00 48.43 A C ATOM 3627 N19 LIG C 1 22.023 33.989 31.739 1.00 42.50 A N ATOM 3628 C20 LIG C 1 18.588 40.255 32.553 1.00 59.78 A C ATOM 3629 N21 LIG C 1 17.265 40.099 32.948 1.00 61.09 A N ATOM 3630 O22 LIG C 1 19.264 40.992 33.279 1.00 56.39 A O END

TABLE 13 Coordinates for proMMP9(35-444 ΔFnII) (SEQ ID NO: 12) complex with Example 3 ATOM 1 N THR A 40 3.707 63.329 27.801 1.00 65.23 A N ATOM 2 CA THR A 40 5.111 63.406 27.409 1.00 56.43 A C ATOM 3 C THR A 40 5.284 63.878 25.958 1.00 57.40 A C ATOM 4 CB THR A 40 5.845 62.067 27.633 1.00 47.95 A C ATOM 5 OG1 THR A 40 7.241 62.314 27.838 1.00 57.95 A O ATOM 6 CG2 THR A 40 5.661 61.147 26.439 1.00 44.46 A C ATOM 7 O THR A 40 6.406 64.094 25.499 1.00 63.74 A O ATOM 8 CB ASP A 41 2.876 64.686 23.248 1.00 48.39 A C ATOM 9 CG ASP A 41 2.712 63.464 22.366 1.00 54.52 A C ATOM 10 OD1 ASP A 41 3.690 62.694 22.225 1.00 51.80 A O ATOM 11 OD2 ASP A 41 1.610 63.279 21.804 1.00 53.68 A O ATOM 12 C ASP A 41 4.631 66.150 24.272 1.00 52.10 A C ATOM 13 O ASP A 41 5.612 66.667 23.751 1.00 51.97 A O ATOM 14 N ASP A 41 4.182 64.024 25.230 1.00 51.04 A N ATOM 15 CA ASP A 41 4.231 64.721 23.952 1.00 53.17 A C ATOM 16 N ARG A 42 3.863 66.771 25.155 1.00 49.17 A N ATOM 17 CA ARG A 42 4.240 68.030 25.777 1.00 52.85 A C ATOM 18 CB ARG A 42 3.368 68.245 27.023 1.00 41.01 A C ATOM 19 CG ARG A 42 3.845 69.335 27.960 1.00 53.00 A C ATOM 20 CD ARG A 42 3.256 70.701 27.619 1.00 50.04 A C ATOM 21 NE ARG A 42 3.930 71.767 28.356 1.00 49.06 A N ATOM 22 CZ ARG A 42 3.431 72.983 28.562 1.00 51.93 A C ATOM 23 NH1 ARG A 42 2.225 73.308 28.105 1.00 53.17 A N ATOM 24 NH2 ARG A 42 4.144 73.875 29.233 1.00 47.20 A N ATOM 25 C ARG A 42 5.734 68.051 26.152 1.00 49.50 A C ATOM 26 O ARG A 42 6.405 69.071 25.997 1.00 44.17 A O ATOM 27 N GLN A 43 6.238 66.919 26.642 1.00 51.53 A N ATOM 28 CA GLN A 43 7.625 66.782 27.102 1.00 48.90 A C ATOM 29 CB GLN A 43 7.793 65.464 27.868 1.00 54.47 A C ATOM 30 CG GLN A 43 7.214 65.410 29.305 1.00 62.36 A C ATOM 31 CD GLN A 43 5.885 66.144 29.493 1.00 65.21 A C ATOM 32 OE1 GLN A 43 4.865 65.789 28.894 1.00 63.86 A O ATOM 33 NE2 GLN A 43 5.892 67.162 30.351 1.00 58.16 A N ATOM 34 C GLN A 43 8.592 66.797 25.917 1.00 51.40 A C ATOM 35 O GLN A 43 9.657 67.409 25.962 1.00 47.08 A O ATOM 36 N LEU A 44 8.201 66.098 24.858 1.00 53.65 A N ATOM 37 CA LEU A 44 8.953 66.048 23.617 1.00 45.75 A C ATOM 38 CB LEU A 44 8.167 65.224 22.603 1.00 45.32 A C ATOM 39 CG LEU A 44 8.902 64.533 21.466 1.00 38.28 A C ATOM 40 CD1 LEU A 44 9.509 63.235 21.970 1.00 39.36 A C ATOM 41 CD2 LEU A 44 7.938 64.266 20.328 1.00 37.71 A C ATOM 42 C LEU A 44 9.173 67.453 23.062 1.00 40.29 A C ATOM 43 O LEU A 44 10.231 67.758 22.526 1.00 43.14 A O ATOM 44 N ALA A 45 8.165 68.304 23.200 1.00 37.38 A N ATOM 45 CA ALA A 45 8.202 69.650 22.647 1.00 38.15 A C ATOM 46 CB ALA A 45 6.812 70.232 22.602 1.00 40.95 A C ATOM 47 C ALA A 45 9.141 70.580 23.410 1.00 44.99 A C ATOM 48 O ALA A 45 9.820 71.414 22.815 1.00 46.69 A O ATOM 49 N GLU A 46 9.191 70.433 24.726 1.00 45.22 A N ATOM 50 CA GLU A 46 10.050 71.285 25.538 1.00 44.34 A C ATOM 51 CB GLU A 46 9.692 71.124 27.019 1.00 44.15 A C ATOM 52 CG GLU A 46 8.385 71.828 27.386 1.00 47.21 A C ATOM 53 CD GLU A 46 7.645 71.193 28.563 1.00 58.84 A C ATOM 54 OE1 GLU A 46 8.281 70.551 29.428 1.00 66.08 A O ATOM 55 OE2 GLU A 46 6.409 71.350 28.627 1.00 57.46 A O ATOM 56 C GLU A 46 11.540 71.018 25.283 1.00 44.91 A C ATOM 57 O GLU A 46 12.347 71.950 25.183 1.00 43.32 A O ATOM 58 N GLU A 47 11.887 69.740 25.171 1.00 41.42 A N ATOM 59 CA GLU A 47 13.264 69.311 24.987 1.00 43.32 A C ATOM 60 CB GLU A 47 13.383 67.812 25.301 1.00 49.05 A C ATOM 61 CG GLU A 47 14.672 67.144 24.839 1.00 51.28 A C ATOM 62 CD GLU A 47 15.921 67.781 25.426 1.00 59.60 A C ATOM 63 OE1 GLU A 47 15.867 68.273 26.578 1.00 61.96 A O ATOM 64 OE2 GLU A 47 16.961 67.786 24.731 1.00 54.90 A O ATOM 65 C GLU A 47 13.710 69.605 23.561 1.00 48.70 A C ATOM 66 O GLU A 47 14.872 69.925 23.303 1.00 44.84 A O ATOM 67 N TYR A 48 12.767 69.511 22.635 1.00 47.27 A N ATOM 68 CA TYR A 48 13.035 69.817 21.243 1.00 36.23 A C ATOM 69 CB TYR A 48 11.916 69.259 20.389 1.00 38.13 A C ATOM 70 CG TYR A 48 12.139 69.351 18.914 1.00 34.88 A C ATOM 71 CD1 TYR A 48 12.052 70.572 18.248 1.00 34.98 A C ATOM 72 CE1 TYR A 48 12.240 70.647 16.876 1.00 36.21 A C ATOM 73 CD2 TYR A 48 12.393 68.213 18.171 1.00 33.55 A C ATOM 74 CE2 TYR A 48 12.580 68.279 16.809 1.00 32.78 A C ATOM 75 CZ TYR A 48 12.502 69.494 16.165 1.00 31.59 A C ATOM 76 OH TYR A 48 12.690 69.542 14.809 1.00 34.86 A O ATOM 77 C TYR A 48 13.126 71.317 21.044 1.00 40.70 A C ATOM 78 O TYR A 48 14.001 71.798 20.336 1.00 46.73 A O ATOM 79 N LEU A 49 12.220 72.070 21.650 1.00 39.93 A N ATOM 80 CA LEU A 49 12.303 73.515 21.518 1.00 42.14 A C ATOM 81 CB LEU A 49 11.097 74.204 22.142 1.00 40.66 A C ATOM 82 CG LEU A 49 9.752 74.009 21.448 1.00 40.53 A C ATOM 83 CD1 LEU A 49 8.636 74.595 22.310 1.00 36.70 A C ATOM 84 CD2 LEU A 49 9.769 74.625 20.066 1.00 36.54 A C ATOM 85 C LEU A 49 13.582 74.009 22.172 1.00 43.88 A C ATOM 86 O LEU A 49 14.243 74.921 21.664 1.00 41.86 A O ATOM 87 N TYR A 50 13.941 73.410 23.301 1.00 45.31 A N ATOM 88 CA TYR A 50 15.121 73.882 24.013 1.00 44.52 A C ATOM 89 CB TYR A 50 15.235 73.292 25.428 1.00 39.30 A C ATOM 90 CG TYR A 50 16.641 73.371 25.971 1.00 38.74 A C ATOM 91 CD1 TYR A 50 17.109 74.527 26.583 1.00 42.78 A C ATOM 92 CE1 TYR A 50 18.408 74.611 27.061 1.00 38.89 A C ATOM 93 CD2 TYR A 50 17.518 72.298 25.833 1.00 46.42 A C ATOM 94 CE2 TYR A 50 18.821 72.370 26.303 1.00 42.93 A C ATOM 95 CZ TYR A 50 19.257 73.529 26.919 1.00 45.61 A C ATOM 96 OH TYR A 50 20.549 73.600 27.390 1.00 52.91 A O ATOM 97 C TYR A 50 16.340 73.537 23.195 1.00 38.67 A C ATOM 98 O TYR A 50 17.150 74.399 22.882 1.00 41.01 A O ATOM 99 N ARG A 51 16.438 72.263 22.838 1.00 41.08 A N ATOM 100 CA ARG A 51 17.605 71.724 22.160 1.00 37.70 A C ATOM 101 CB ARG A 51 17.371 70.255 21.805 1.00 35.94 A C ATOM 102 CG ARG A 51 18.378 69.677 20.844 1.00 40.07 A C ATOM 103 CD ARG A 51 17.995 68.272 20.403 1.00 40.13 A C ATOM 104 NE ARG A 51 18.320 67.268 21.413 1.00 44.72 A N ATOM 105 CZ ARG A 51 19.548 66.813 21.647 1.00 44.49 A C ATOM 106 NH1 ARG A 51 20.572 67.286 20.944 1.00 45.84 A N ATOM 107 NH2 ARG A 51 19.756 65.896 22.589 1.00 36.35 A N ATOM 108 C ARG A 51 17.978 72.510 20.909 1.00 42.20 A C ATOM 109 O ARG A 51 19.153 72.815 20.698 1.00 48.01 A O ATOM 110 N TYR A 52 16.991 72.845 20.084 1.00 34.17 A N ATOM 111 CA TYR A 52 17.291 73.442 18.789 1.00 35.47 A C ATOM 112 CB TYR A 52 16.398 72.841 17.708 1.00 35.15 A C ATOM 113 CG TYR A 52 16.722 71.388 17.508 1.00 34.30 A C ATOM 114 CD1 TYR A 52 15.791 70.411 17.776 1.00 34.22 A C ATOM 115 CE1 TYR A 52 16.093 69.080 17.622 1.00 35.92 A C ATOM 116 CD2 TYR A 52 17.991 70.993 17.107 1.00 35.72 A C ATOM 117 CE2 TYR A 52 18.309 69.660 16.949 1.00 34.68 A C ATOM 118 CZ TYR A 52 17.351 68.709 17.207 1.00 40.38 A C ATOM 119 OH TYR A 52 17.645 67.377 17.058 1.00 42.46 A O ATOM 120 C TYR A 52 17.323 74.971 18.742 1.00 39.45 A C ATOM 121 O TYR A 52 17.451 75.562 17.667 1.00 36.86 A O ATOM 122 N GLY A 53 17.234 75.605 19.909 1.00 38.15 A N ATOM 123 CA GLY A 53 17.515 77.028 20.020 1.00 37.95 A C ATOM 124 C GLY A 53 16.310 77.936 20.156 1.00 42.61 A C ATOM 125 O GLY A 53 16.452 79.141 20.332 1.00 47.74 A O ATOM 126 N TYR A 54 15.120 77.352 20.103 1.00 46.81 A N ATOM 127 CA TYR A 54 13.881 78.124 20.086 1.00 45.99 A C ATOM 128 CB TYR A 54 12.750 77.251 19.573 1.00 40.94 A C ATOM 129 CG TYR A 54 13.018 76.671 18.213 1.00 39.27 A C ATOM 130 CD1 TYR A 54 13.372 75.340 18.066 1.00 36.86 A C ATOM 131 CE1 TYR A 54 13.607 74.804 16.826 1.00 37.65 A C ATOM 132 CD2 TYR A 54 12.911 77.454 17.073 1.00 37.01 A C ATOM 133 CE2 TYR A 54 13.145 76.927 15.828 1.00 38.04 A C ATOM 134 CZ TYR A 54 13.491 75.604 15.714 1.00 37.87 A C ATOM 135 OH TYR A 54 13.723 75.078 14.480 1.00 41.55 A O ATOM 136 C TYR A 54 13.480 78.768 21.419 1.00 45.13 A C ATOM 137 O TYR A 54 13.330 79.983 21.496 1.00 48.34 A O ATOM 138 N THR A 55 13.283 77.957 22.451 1.00 39.98 A N ATOM 139 CA THR A 55 12.883 78.475 23.749 1.00 42.41 A C ATOM 140 CB THR A 55 12.871 77.379 24.818 1.00 36.38 A C ATOM 141 OG1 THR A 55 14.215 77.073 25.189 1.00 40.11 A O ATOM 142 CG2 THR A 55 12.225 76.137 24.290 1.00 42.64 A C ATOM 143 C THR A 55 13.821 79.579 24.229 1.00 53.13 A C ATOM 144 O THR A 55 13.397 80.471 24.967 1.00 51.47 A O ATOM 145 N ARG A 56 15.088 79.511 23.809 1.00 49.05 A N ATOM 146 CA ARG A 56 16.118 80.454 24.248 1.00 45.72 A C ATOM 147 CB ARG A 56 17.508 79.927 23.874 1.00 44.73 A C ATOM 148 CG ARG A 56 17.645 78.396 23.966 1.00 54.70 A C ATOM 149 CD ARG A 56 18.930 77.900 23.294 1.00 61.19 A C ATOM 150 NE ARG A 56 19.387 76.606 23.808 1.00 64.09 A N ATOM 151 CZ ARG A 56 20.237 75.792 23.178 1.00 57.07 A C ATOM 152 NH1 ARG A 56 20.725 76.115 21.987 1.00 57.51 A N ATOM 153 NH2 ARG A 56 20.592 74.640 23.736 1.00 45.98 A N ATOM 154 C ARG A 56 15.887 81.835 23.630 1.00 50.10 A C ATOM 155 O ARG A 56 15.978 82.858 24.306 1.00 52.08 A O ATOM 156 N VAL A 57 15.585 81.847 22.336 1.00 51.08 A N ATOM 157 CA VAL A 57 15.222 83.060 21.625 1.00 49.27 A C ATOM 158 CB VAL A 57 15.099 82.789 20.103 1.00 56.69 A C ATOM 159 CG1 VAL A 57 14.731 84.064 19.340 1.00 54.91 A C ATOM 160 CG2 VAL A 57 16.394 82.194 19.566 1.00 43.94 A C ATOM 161 C VAL A 57 13.899 83.589 22.174 1.00 49.15 A C ATOM 162 O VAL A 57 13.679 84.796 22.227 1.00 52.68 A O ATOM 163 N GLY A 58 13.025 82.675 22.584 1.00 47.80 A N ATOM 164 CA GLY A 58 11.768 83.037 23.215 1.00 44.98 A C ATOM 165 C GLY A 58 12.023 83.814 24.491 1.00 53.75 A C ATOM 166 O GLY A 58 11.510 84.919 24.671 1.00 53.91 A O ATOM 167 N GLU A 59 12.826 83.234 25.379 1.00 51.54 A N ATOM 168 CA GLU A 59 13.218 83.901 26.615 1.00 49.19 A C ATOM 169 C GLU A 59 13.735 85.282 26.300 1.00 55.60 A C ATOM 170 CB GLU A 59 14.347 83.132 27.296 1.00 47.68 A C ATOM 171 CG GLU A 59 14.141 81.643 27.349 1.00 50.21 A C ATOM 172 CD GLU A 59 15.143 80.961 28.245 1.00 58.44 A C ATOM 173 OE1 GLU A 59 16.266 81.495 28.394 1.00 56.06 A O ATOM 174 OE2 GLU A 59 14.806 79.895 28.802 1.00 62.38 A O ATOM 175 O GLU A 59 13.220 86.292 26.782 1.00 54.05 A O ATOM 176 N MET A 60 14.777 85.288 25.474 1.00 57.94 A N ATOM 177 CA MET A 60 15.540 86.467 25.103 1.00 53.60 A C ATOM 178 C MET A 60 14.707 87.434 24.255 1.00 57.73 A C ATOM 179 CB MET A 60 16.770 85.983 24.335 1.00 52.36 A C ATOM 180 CG MET A 60 17.784 87.027 23.942 1.00 55.17 A C ATOM 181 SD MET A 60 18.841 86.339 22.662 1.00 52.76 A S ATOM 182 CE MET A 60 19.242 84.752 23.384 1.00 48.99 A C ATOM 183 O MET A 60 15.226 88.095 23.357 1.00 63.84 A O ATOM 184 N ARG A 61 13.419 87.528 24.570 1.00 55.96 A N ATOM 185 CA ARG A 61 12.448 88.220 23.730 1.00 56.54 A C ATOM 186 C ARG A 61 11.158 88.410 24.534 1.00 60.43 A C ATOM 187 CB ARG A 61 12.182 87.383 22.481 1.00 54.80 A C ATOM 188 CG ARG A 61 11.736 88.146 21.253 1.00 59.48 A C ATOM 189 CD ARG A 61 12.204 87.421 19.990 1.00 57.07 A C ATOM 190 NE ARG A 61 11.202 87.438 18.926 1.00 58.22 A N ATOM 191 CZ ARG A 61 11.414 87.004 17.685 1.00 64.87 A C ATOM 192 NH1 ARG A 61 10.435 87.055 16.789 1.00 61.16 A N ATOM 193 NH2 ARG A 61 12.605 86.523 17.337 1.00 61.86 A N ATOM 194 O ARG A 61 10.160 88.936 24.031 1.00 53.44 A O ATOM 195 N GLY A 62 11.197 87.957 25.787 1.00 53.17 A N ATOM 196 CA GLY A 62 10.123 88.171 26.741 1.00 60.34 A C ATOM 197 C GLY A 62 9.047 87.098 26.791 1.00 61.87 A C ATOM 198 O GLY A 62 8.042 87.270 27.474 1.00 59.04 A O ATOM 199 N GLU A 63 9.264 85.986 26.093 1.00 62.54 A N ATOM 200 CA GLU A 63 8.200 85.009 25.873 1.00 59.19 A C ATOM 201 C GLU A 63 8.506 83.570 26.294 1.00 61.94 A C ATOM 202 CB GLU A 63 7.785 85.023 24.404 1.00 58.65 A C ATOM 203 CG GLU A 63 7.089 86.292 23.961 1.00 57.73 A C ATOM 204 CD GLU A 63 7.172 86.491 22.462 1.00 61.60 A C ATOM 205 OE1 GLU A 63 8.286 86.370 21.909 1.00 67.13 A O ATOM 206 OE2 GLU A 63 6.131 86.776 21.836 1.00 62.49 A O ATOM 207 O GLU A 63 8.559 82.673 25.459 1.00 59.46 A O ATOM 208 N SER A 64 8.681 83.353 27.594 1.00 71.87 A N ATOM 209 CA SER A 64 8.763 82.006 28.153 1.00 66.90 A C ATOM 210 C SER A 64 7.548 81.809 29.057 1.00 60.96 A C ATOM 211 CB SER A 64 10.069 81.830 28.929 1.00 70.73 A C ATOM 212 OG SER A 64 10.329 82.952 29.759 1.00 72.39 A O ATOM 213 O SER A 64 7.672 81.640 30.268 1.00 51.29 A O ATOM 214 N LYS A 65 6.375 81.802 28.432 1.00 66.64 A N ATOM 215 CA LYS A 65 5.108 82.112 29.084 1.00 65.93 A C ATOM 216 C LYS A 65 4.017 81.243 28.474 1.00 72.49 A C ATOM 217 CB LYS A 65 4.780 83.555 28.736 1.00 61.06 A C ATOM 218 CG LYS A 65 5.005 83.818 27.239 1.00 58.47 A C ATOM 219 CD LYS A 65 5.102 85.283 26.908 1.00 60.32 A C ATOM 220 CE LYS A 65 3.817 85.805 26.318 1.00 65.09 A C ATOM 221 NZ LYS A 65 3.809 87.291 26.344 1.00 70.67 A N ATOM 222 O LYS A 65 3.080 81.765 27.856 1.00 68.17 A O ATOM 223 N SER A 66 4.130 79.930 28.652 1.00 65.46 A N ATOM 224 CA SER A 66 3.504 78.993 27.728 1.00 61.84 A C ATOM 225 C SER A 66 4.508 78.806 26.589 1.00 62.00 A C ATOM 226 CB SER A 66 2.168 79.530 27.213 1.00 53.77 A C ATOM 227 OG SER A 66 2.067 79.390 25.811 1.00 60.68 A O ATOM 228 O SER A 66 5.559 79.453 26.573 1.00 55.56 A O ATOM 229 N LEU A 67 4.201 77.925 25.648 1.00 57.21 A N ATOM 230 CA LEU A 67 5.158 77.597 24.604 1.00 54.60 A C ATOM 231 C LEU A 67 4.724 78.157 23.258 1.00 49.73 A C ATOM 232 CB LEU A 67 5.340 76.077 24.503 1.00 51.02 A C ATOM 233 CG LEU A 67 6.051 75.307 25.621 1.00 48.25 A C ATOM 234 CD1 LEU A 67 5.685 75.802 27.023 1.00 53.44 A C ATOM 235 CD2 LEU A 67 5.737 73.826 25.472 1.00 44.47 A C ATOM 236 O LEU A 67 5.334 77.853 22.239 1.00 44.39 A O ATOM 237 N GLY A 68 3.671 78.971 23.257 1.00 56.41 A N ATOM 238 CA GLY A 68 3.156 79.533 22.022 1.00 52.56 A C ATOM 239 C GLY A 68 4.252 80.149 21.182 1.00 48.73 A C ATOM 240 O GLY A 68 4.491 79.725 20.051 1.00 51.09 A O ATOM 241 N PRO A 69 4.938 81.152 21.739 1.00 52.52 A N ATOM 242 CD PRO A 69 4.705 81.745 23.066 1.00 52.37 A C ATOM 243 CA PRO A 69 5.993 81.854 21.008 1.00 44.37 A C ATOM 244 CB PRO A 69 6.572 82.794 22.065 1.00 53.19 A C ATOM 245 CG PRO A 69 5.437 83.054 22.976 1.00 54.17 A C ATOM 246 C PRO A 69 7.061 80.911 20.466 1.00 44.95 A C ATOM 247 O PRO A 69 7.338 80.958 19.268 1.00 52.80 A O ATOM 248 N ALA A 70 7.646 80.072 21.317 1.00 47.10 A N ATOM 249 CA ALA A 70 8.710 79.166 20.881 1.00 40.79 A C ATOM 250 CB ALA A 70 9.208 78.324 22.034 1.00 38.89 A C ATOM 251 C ALA A 70 8.237 78.278 19.736 1.00 46.20 A C ATOM 252 O ALA A 70 8.973 78.039 18.782 1.00 46.93 A O ATOM 253 N LEU A 71 7.003 77.800 19.837 1.00 42.27 A N ATOM 254 CA LEU A 71 6.393 77.027 18.771 1.00 44.29 A C ATOM 255 CB LEU A 71 4.963 76.645 19.144 1.00 42.21 A C ATOM 256 CG LEU A 71 4.844 75.574 20.219 1.00 38.82 A C ATOM 257 CD1 LEU A 71 3.438 75.547 20.809 1.00 41.13 A C ATOM 258 CD2 LEU A 71 5.233 74.229 19.639 1.00 34.24 A C ATOM 259 C LEU A 71 6.370 77.835 17.488 1.00 47.61 A C ATOM 260 O LEU A 71 6.820 77.370 16.439 1.00 47.28 A O ATOM 261 N LEU A 72 5.836 79.048 17.576 1.00 48.24 A N ATOM 262 CA LEU A 72 5.681 79.885 16.397 1.00 46.29 A C ATOM 263 CB LEU A 72 5.092 81.249 16.767 1.00 48.28 A C ATOM 264 CG LEU A 72 4.490 82.110 15.650 1.00 47.91 A C ATOM 265 CD1 LEU A 72 3.097 81.631 15.273 1.00 39.63 A C ATOM 266 CD2 LEU A 72 4.448 83.570 16.075 1.00 41.74 A C ATOM 267 C LEU A 72 7.031 80.032 15.713 1.00 46.30 A C ATOM 268 O LEU A 72 7.120 79.991 14.487 1.00 48.18 A O ATOM 269 N LEU A 73 8.085 80.175 16.508 1.00 47.36 A N ATOM 270 CA LEU A 73 9.426 80.315 15.953 1.00 46.67 A C ATOM 271 CB LEU A 73 10.445 80.638 17.044 1.00 44.51 A C ATOM 272 CG LEU A 73 10.371 81.989 17.751 1.00 49.16 A C ATOM 273 CD1 LEU A 73 11.323 81.992 18.935 1.00 54.05 A C ATOM 274 CD2 LEU A 73 10.682 83.138 16.801 1.00 44.48 A C ATOM 275 C LEU A 73 9.823 79.030 15.240 1.00 51.69 A C ATOM 276 O LEU A 73 10.521 79.055 14.218 1.00 46.37 A O ATOM 277 N LEU A 74 9.384 77.902 15.784 1.00 46.06 A N ATOM 278 CA LEU A 74 9.675 76.632 15.149 1.00 41.97 A C ATOM 279 CB LEU A 74 9.329 75.465 16.075 1.00 42.09 A C ATOM 280 CG LEU A 74 9.562 74.031 15.592 1.00 41.73 A C ATOM 281 CD1 LEU A 74 9.754 73.109 16.775 1.00 36.01 A C ATOM 282 CD2 LEU A 74 8.393 73.548 14.742 1.00 43.31 A C ATOM 283 C LEU A 74 8.900 76.557 13.846 1.00 44.15 A C ATOM 284 O LEU A 74 9.457 76.227 12.806 1.00 43.84 A O ATOM 285 N GLN A 75 7.614 76.889 13.900 1.00 45.23 A N ATOM 286 CA GLN A 75 6.742 76.711 12.744 1.00 41.99 A C ATOM 287 CB GLN A 75 5.307 77.069 13.108 1.00 40.56 A C ATOM 288 CG GLN A 75 4.529 75.897 13.681 1.00 43.57 A C ATOM 289 CD GLN A 75 3.625 76.285 14.835 1.00 42.71 A C ATOM 290 OE1 GLN A 75 2.987 77.347 14.828 1.00 39.21 A O ATOM 291 NE2 GLN A 75 3.569 75.420 15.839 1.00 37.01 A N ATOM 292 C GLN A 75 7.203 77.478 11.503 1.00 44.30 A C ATOM 293 O GLN A 75 7.018 77.028 10.369 1.00 36.77 A O ATOM 294 N LYS A 76 7.811 78.635 11.713 1.00 42.66 A N ATOM 295 CA LYS A 76 8.264 79.414 10.584 1.00 38.57 A C ATOM 296 CB LYS A 76 8.047 80.901 10.837 1.00 37.77 A C ATOM 297 CG LYS A 76 9.137 81.562 11.635 1.00 47.53 A C ATOM 298 CD LYS A 76 8.702 82.950 12.067 1.00 55.62 A C ATOM 299 CE LYS A 76 7.307 82.906 12.687 1.00 51.90 A C ATOM 300 NZ LYS A 76 7.133 83.934 13.738 1.00 48.00 A N ATOM 301 C LYS A 76 9.723 79.089 10.256 1.00 45.83 A C ATOM 302 O LYS A 76 10.206 79.408 9.169 1.00 42.00 A O ATOM 303 N GLN A 77 10.413 78.434 11.188 1.00 45.01 A N ATOM 304 CA GLN A 77 11.765 77.936 10.937 1.00 38.91 A C ATOM 305 CB GLN A 77 12.488 77.632 12.250 1.00 44.46 A C ATOM 306 CG GLN A 77 13.946 77.217 12.084 1.00 42.93 A C ATOM 307 CD GLN A 77 14.792 78.311 11.457 1.00 45.59 A C ATOM 308 OE1 GLN A 77 14.518 79.494 11.642 1.00 40.71 A O ATOM 309 NE2 GLN A 77 15.821 77.918 10.706 1.00 38.13 A N ATOM 310 C GLN A 77 11.766 76.685 10.065 1.00 41.36 A C ATOM 311 O GLN A 77 12.745 76.414 9.363 1.00 43.69 A O ATOM 312 N LEU A 78 10.678 75.919 10.108 1.00 38.12 A N ATOM 313 CA LEU A 78 10.592 74.685 9.326 1.00 40.35 A C ATOM 314 CB LEU A 78 10.240 73.488 10.209 1.00 34.67 A C ATOM 315 CG LEU A 78 11.131 73.169 11.405 1.00 38.97 A C ATOM 316 CD1 LEU A 78 10.377 72.316 12.408 1.00 36.89 A C ATOM 317 CD2 LEU A 78 12.394 72.473 10.964 1.00 40.72 A C ATOM 318 C LEU A 78 9.572 74.807 8.202 1.00 42.99 A C ATOM 319 O LEU A 78 9.306 73.842 7.477 1.00 41.21 A O ATOM 320 N SER A 79 9.005 75.999 8.061 1.00 41.64 A N ATOM 321 CA SER A 79 7.973 76.243 7.057 1.00 39.68 A C ATOM 322 CB SER A 79 8.511 76.008 5.644 1.00 41.37 A C ATOM 323 OG SER A 79 9.484 76.990 5.307 1.00 42.49 A O ATOM 324 C SER A 79 6.721 75.414 7.322 1.00 40.28 A C ATOM 325 O SER A 79 6.159 74.795 6.417 1.00 43.37 A O ATOM 326 N LEU A 80 6.302 75.405 8.584 1.00 41.47 A N ATOM 327 CA LEU A 80 5.019 74.838 8.984 1.00 36.49 A C ATOM 328 CB LEU A 80 5.170 74.045 10.281 1.00 35.90 A C ATOM 329 CG LEU A 80 6.199 72.910 10.326 1.00 37.28 A C ATOM 330 CD1 LEU A 80 6.037 72.099 11.606 1.00 45.14 A C ATOM 331 CD2 LEU A 80 6.067 72.006 9.122 1.00 36.95 A C ATOM 332 C LEU A 80 4.048 75.996 9.183 1.00 37.89 A C ATOM 333 O LEU A 80 4.482 77.124 9.432 1.00 46.12 A O ATOM 334 N PRO A 81 2.737 75.740 9.050 1.00 34.45 A N ATOM 335 CD PRO A 81 2.099 74.500 8.578 1.00 34.04 A C ATOM 336 CA PRO A 81 1.755 76.810 9.283 1.00 35.92 A C ATOM 337 CB PRO A 81 0.411 76.099 9.122 1.00 26.58 A C ATOM 338 CG PRO A 81 0.705 74.954 8.216 1.00 36.31 A C ATOM 339 C PRO A 81 1.884 77.393 10.682 1.00 39.62 A C ATOM 340 O PRO A 81 1.992 76.654 11.666 1.00 41.86 A O ATOM 341 N GLU A 82 1.876 78.715 10.770 1.00 41.52 A N ATOM 342 CA GLU A 82 2.152 79.380 12.041 1.00 46.69 A C ATOM 343 CB GLU A 82 2.876 80.706 11.792 1.00 47.67 A C ATOM 344 CG GLU A 82 4.288 80.492 11.259 1.00 39.26 A C ATOM 345 CD GLU A 82 4.626 81.374 10.067 1.00 53.08 A C ATOM 346 OE1 GLU A 82 4.754 82.606 10.244 1.00 53.45 A O ATOM 347 OE2 GLU A 82 4.785 80.827 8.952 1.00 52.78 A O ATOM 348 C GLU A 82 0.893 79.529 12.898 1.00 47.19 A C ATOM 349 O GLU A 82 0.006 80.340 12.615 1.00 46.15 A O ATOM 350 N THR A 83 0.818 78.708 13.941 1.00 47.88 A N ATOM 351 CA THR A 83 −0.410 78.563 14.713 1.00 41.85 A C ATOM 352 CB THR A 83 −0.992 77.147 14.564 1.00 39.04 A C ATOM 353 OG1 THR A 83 −0.123 76.203 15.204 1.00 39.94 A O ATOM 354 CG2 THR A 83 −1.142 76.780 13.099 1.00 39.15 A C ATOM 355 C THR A 83 −0.179 78.807 16.190 1.00 41.05 A C ATOM 356 O THR A 83 −1.128 79.012 16.942 1.00 44.79 A O ATOM 357 N GLY A 84 1.080 78.768 16.609 1.00 39.14 A N ATOM 358 CA GLY A 84 1.409 78.942 18.008 1.00 40.11 A C ATOM 359 C GLY A 84 0.847 77.822 18.858 1.00 42.86 A C ATOM 360 O GLY A 84 0.738 77.947 20.080 1.00 44.14 A O ATOM 361 N GLU A 85 0.492 76.720 18.206 1.00 41.60 A N ATOM 362 CA GLU A 85 −0.072 75.576 18.907 1.00 45.16 A C ATOM 363 CB GLU A 85 −1.525 75.330 18.470 1.00 42.75 A C ATOM 364 CG GLU A 85 −2.426 76.556 18.443 1.00 41.12 A C ATOM 365 CD GLU A 85 −2.875 77.006 19.825 1.00 46.34 A C ATOM 366 OE1 GLU A 85 −2.701 76.241 20.799 1.00 41.93 A O ATOM 367 OE2 GLU A 85 −3.405 78.132 19.932 1.00 44.81 A O ATOM 368 C GLU A 85 0.740 74.306 18.663 1.00 43.44 A C ATOM 369 O GLU A 85 1.125 74.014 17.531 1.00 42.30 A O ATOM 370 N LEU A 86 0.995 73.558 19.732 1.00 40.86 A N ATOM 371 CA LEU A 86 1.474 72.194 19.615 1.00 37.12 A C ATOM 372 CB LEU A 86 1.751 71.595 20.996 1.00 32.50 A C ATOM 373 CG LEU A 86 2.253 70.145 21.098 1.00 33.94 A C ATOM 374 CD1 LEU A 86 3.431 69.888 20.177 1.00 37.84 A C ATOM 375 CD2 LEU A 86 2.621 69.784 22.535 1.00 34.35 A C ATOM 376 C LEU A 86 0.364 71.426 18.927 1.00 43.66 A C ATOM 377 O LEU A 86 −0.450 70.775 19.582 1.00 44.05 A O ATOM 378 N ASP A 87 0.317 71.521 17.602 1.00 44.33 A N ATOM 379 CA ASP A 87 −0.721 70.850 16.836 1.00 39.30 A C ATOM 380 CB ASP A 87 −1.364 71.825 15.858 1.00 38.35 A C ATOM 381 CG ASP A 87 −0.345 72.563 15.018 1.00 43.68 A C ATOM 382 OD1 ASP A 87 0.785 72.056 14.886 1.00 44.30 A O ATOM 383 OD2 ASP A 87 −0.673 73.645 14.484 1.00 43.81 A O ATOM 384 C ASP A 87 −0.175 69.617 16.115 1.00 42.17 A C ATOM 385 O ASP A 87 0.998 69.265 16.266 1.00 38.75 A O ATOM 386 N SER A 88 −1.035 68.959 15.344 1.00 41.03 A N ATOM 387 CA SER A 88 −0.663 67.722 14.660 1.00 44.22 A C ATOM 388 CB SER A 88 −1.838 67.168 13.844 1.00 44.49 A C ATOM 389 OG SER A 88 −2.694 66.373 14.648 1.00 44.75 A O ATOM 390 C SER A 88 0.557 67.883 13.765 1.00 40.43 A C ATOM 391 O SER A 88 1.443 67.032 13.767 1.00 41.50 A O ATOM 392 N ALA A 89 0.600 68.967 12.997 1.00 35.28 A N ATOM 393 CA ALA A 89 1.719 69.195 12.092 1.00 34.20 A C ATOM 394 CB ALA A 89 1.454 70.378 11.179 1.00 26.35 A C ATOM 395 C ALA A 89 3.003 69.417 12.864 1.00 36.73 A C ATOM 396 O ALA A 89 4.073 68.988 12.439 1.00 41.09 A O ATOM 397 N THR A 90 2.899 70.089 14.001 1.00 34.29 A N ATOM 398 CA THR A 90 4.090 70.460 14.747 1.00 35.74 A C ATOM 399 CB THR A 90 3.832 71.680 15.632 1.00 36.64 A C ATOM 400 OG1 THR A 90 3.580 72.820 14.797 1.00 36.02 A O ATOM 401 CG2 THR A 90 5.023 71.948 16.531 1.00 31.50 A C ATOM 402 C THR A 90 4.675 69.305 15.555 1.00 36.10 A C ATOM 403 O THR A 90 5.892 69.205 15.707 1.00 34.37 A O ATOM 404 N LEU A 91 3.811 68.424 16.050 1.00 39.61 A N ATOM 405 CA LEU A 91 4.266 67.251 16.796 1.00 38.55 A C ATOM 406 CB LEU A 91 3.153 66.678 17.677 1.00 38.66 A C ATOM 407 CG LEU A 91 3.515 65.476 18.560 1.00 46.50 A C ATOM 408 CD1 LEU A 91 4.836 65.676 19.301 1.00 40.95 A C ATOM 409 CD2 LEU A 91 2.392 65.184 19.539 1.00 43.02 A C ATOM 410 C LEU A 91 4.792 66.199 15.834 1.00 39.88 A C ATOM 411 O LEU A 91 5.803 65.547 16.100 1.00 43.03 A O ATOM 412 N LYS A 92 4.109 66.042 14.709 1.00 37.79 A N ATOM 413 CA LYS A 92 4.614 65.180 13.654 1.00 38.93 A C ATOM 414 CB LYS A 92 3.788 65.368 12.381 1.00 42.69 A C ATOM 415 CG LYS A 92 4.378 64.754 11.130 1.00 38.78 A C ATOM 416 CD LYS A 92 3.413 64.896 9.962 1.00 52.75 A C ATOM 417 CE LYS A 92 3.911 64.149 8.724 1.00 60.93 A C ATOM 418 NZ LYS A 92 2.860 64.036 7.665 1.00 61.49 A N ATOM 419 C LYS A 92 6.078 65.539 13.407 1.00 42.82 A C ATOM 420 O LYS A 92 6.970 64.710 13.595 1.00 45.15 A O ATOM 421 N ALA A 93 6.310 66.788 13.005 1.00 39.05 A N ATOM 422 CA ALA A 93 7.652 67.310 12.755 1.00 40.24 A C ATOM 423 CB ALA A 93 7.597 68.828 12.543 1.00 41.52 A C ATOM 424 C ALA A 93 8.651 66.968 13.863 1.00 38.04 A C ATOM 425 O ALA A 93 9.719 66.431 13.605 1.00 42.76 A O ATOM 426 N MET A 94 8.298 67.287 15.099 1.00 41.25 A N ATOM 427 CA MET A 94 9.168 67.016 16.238 1.00 40.33 A C ATOM 428 CB MET A 94 8.474 67.465 17.535 1.00 39.65 A C ATOM 429 CG MET A 94 8.283 68.968 17.640 1.00 35.07 A C ATOM 430 SD MET A 94 7.436 69.463 19.153 1.00 43.06 A S ATOM 431 CE MET A 94 7.655 71.238 19.182 1.00 29.54 A C ATOM 432 C MET A 94 9.608 65.544 16.337 1.00 37.24 A C ATOM 433 O MET A 94 10.681 65.253 16.853 1.00 39.64 A O ATOM 434 N ARG A 95 8.775 64.630 15.844 1.00 42.55 A N ATOM 435 CA ARG A 95 9.060 63.193 15.871 1.00 37.31 A C ATOM 436 CB ARG A 95 7.761 62.373 15.867 1.00 47.18 A C ATOM 437 CG ARG A 95 7.059 62.199 17.222 1.00 54.29 A C ATOM 438 CD ARG A 95 5.888 61.206 17.110 1.00 46.18 A C ATOM 439 NE ARG A 95 5.024 61.226 18.292 1.00 65.38 A N ATOM 440 CZ ARG A 95 3.735 61.573 18.288 1.00 65.21 A C ATOM 441 NH1 ARG A 95 3.132 61.924 17.157 1.00 60.76 A N ATOM 442 NH2 ARG A 95 3.039 61.560 19.419 1.00 58.47 A N ATOM 443 C ARG A 95 9.868 62.769 14.664 1.00 45.34 A C ATOM 444 O ARG A 95 10.150 61.584 14.486 1.00 50.76 A O ATOM 445 N THR A 96 10.212 63.724 13.808 1.00 45.88 A N ATOM 446 CA THR A 96 11.005 63.408 12.629 1.00 41.71 A C ATOM 447 CB THR A 96 10.732 64.403 11.491 1.00 39.84 A C ATOM 448 OG1 THR A 96 9.431 64.152 10.957 1.00 42.90 A O ATOM 449 CG2 THR A 96 11.742 64.241 10.379 1.00 46.83 A C ATOM 450 C THR A 96 12.499 63.340 12.957 1.00 43.04 A C ATOM 451 O THR A 96 13.011 64.178 13.704 1.00 45.82 A O ATOM 452 N PRO A 97 13.190 62.310 12.429 1.00 45.54 A N ATOM 453 CD PRO A 97 12.565 61.128 11.809 1.00 42.78 A C ATOM 454 CA PRO A 97 14.651 62.173 12.513 1.00 45.20 A C ATOM 455 CB PRO A 97 14.919 60.835 11.818 1.00 36.85 A C ATOM 456 CG PRO A 97 13.630 60.096 11.918 1.00 41.64 A C ATOM 457 C PRO A 97 15.330 63.301 11.752 1.00 43.25 A C ATOM 458 O PRO A 97 14.884 63.658 10.663 1.00 43.49 A O ATOM 459 N ARG A 98 16.397 63.851 12.316 1.00 41.91 A N ATOM 460 CA ARG A 98 16.975 65.066 11.780 1.00 37.38 A C ATOM 461 CB ARG A 98 16.145 66.274 12.218 1.00 36.18 A C ATOM 462 CG ARG A 98 16.084 66.448 13.730 1.00 36.05 A C ATOM 463 CD ARG A 98 15.636 67.854 14.098 1.00 33.12 A C ATOM 464 NE ARG A 98 16.707 68.829 13.948 1.00 35.92 A N ATOM 465 CZ ARG A 98 16.526 70.140 13.804 1.00 35.03 A C ATOM 466 NH1 ARG A 98 15.307 70.658 13.785 1.00 32.81 A N ATOM 467 NH2 ARG A 98 17.574 70.935 13.679 1.00 32.79 A N ATOM 468 C ARG A 98 18.400 65.256 12.255 1.00 36.84 A C ATOM 469 O ARG A 98 18.973 64.379 12.896 1.00 36.01 A O ATOM 470 N CYS A 99 18.941 66.431 11.944 1.00 30.25 A N ATOM 471 CA CYS A 99 20.302 66.801 12.269 1.00 29.21 A C ATOM 472 CB CYS A 99 20.784 67.807 11.235 1.00 29.65 A C ATOM 473 SG CYS A 99 22.438 68.453 11.472 1.00 39.09 A S ATOM 474 C CYS A 99 20.404 67.404 13.672 1.00 36.23 A C ATOM 475 O CYS A 99 19.572 68.217 14.073 1.00 35.02 A O ATOM 476 N GLY A 100 21.439 67.018 14.411 1.00 34.92 A N ATOM 477 CA GLY A 100 21.625 67.501 15.768 1.00 36.71 A C ATOM 478 C GLY A 100 22.009 68.964 15.852 1.00 34.96 A C ATOM 479 O GLY A 100 22.090 69.547 16.940 1.00 31.46 A O ATOM 480 N VAL A 101 22.250 69.567 14.698 1.00 31.30 A N ATOM 481 CA VAL A 101 22.680 70.953 14.665 1.00 34.55 A C ATOM 482 CB VAL A 101 23.280 71.336 13.280 1.00 34.11 A C ATOM 483 CG1 VAL A 101 23.762 72.781 13.277 1.00 36.93 A C ATOM 484 CG2 VAL A 101 24.423 70.434 12.942 1.00 30.91 A C ATOM 485 C VAL A 101 21.504 71.853 15.004 1.00 34.16 A C ATOM 486 O VAL A 101 20.467 71.791 14.345 1.00 39.80 A O ATOM 487 N PRO A 102 21.648 72.672 16.054 1.00 32.79 A N ATOM 488 CD PRO A 102 22.619 72.475 17.142 1.00 36.55 A C ATOM 489 CA PRO A 102 20.676 73.715 16.385 1.00 34.05 A C ATOM 490 CB PRO A 102 21.415 74.532 17.442 1.00 34.33 A C ATOM 491 CG PRO A 102 22.226 73.515 18.156 1.00 33.48 A C ATOM 492 C PRO A 102 20.294 74.597 15.199 1.00 30.76 A C ATOM 493 O PRO A 102 21.170 75.067 14.489 1.00 32.23 A O ATOM 494 N ASP A 103 18.992 74.808 15.005 1.00 34.22 A N ATOM 495 CA ASP A 103 18.460 75.705 13.975 1.00 35.08 A C ATOM 496 CB ASP A 103 16.975 75.434 13.744 1.00 35.75 A C ATOM 497 CG ASP A 103 16.686 73.985 13.525 1.00 36.11 A C ATOM 498 OD1 ASP A 103 17.478 73.330 12.820 1.00 43.71 A O ATOM 499 OD2 ASP A 103 15.674 73.502 14.055 1.00 31.30 A O ATOM 500 C ASP A 103 18.589 77.178 14.326 1.00 34.69 A C ATOM 501 O ASP A 103 18.498 78.038 13.451 1.00 34.52 A O ATOM 502 N LEU A 104 18.760 77.481 15.605 1.00 33.07 A N ATOM 503 CA LEU A 104 18.752 78.875 16.017 1.00 39.54 A C ATOM 504 CB LEU A 104 17.404 79.289 16.630 1.00 40.92 A C ATOM 505 CG LEU A 104 16.449 80.077 15.728 1.00 38.00 A C ATOM 506 CD1 LEU A 104 15.205 80.462 16.499 1.00 42.68 A C ATOM 507 CD2 LEU A 104 17.128 81.326 15.188 1.00 34.79 A C ATOM 508 C LEU A 104 19.883 79.207 16.952 1.00 43.50 A C ATOM 509 O LEU A 104 19.958 78.714 18.077 1.00 41.39 A O ATOM 510 N GLY A 105 20.766 80.063 16.456 1.00 54.30 A N ATOM 511 CA GLY A 105 21.885 80.530 17.231 1.00 57.99 A C ATOM 512 C GLY A 105 22.937 79.486 17.540 1.00 58.30 A C ATOM 513 O GLY A 105 23.255 78.635 16.713 1.00 48.55 A O ATOM 514 N ARG A 106 23.455 79.557 18.762 1.00 63.75 A N ATOM 515 CA ARG A 106 24.797 79.077 19.067 1.00 68.31 A C ATOM 516 CB ARG A 106 25.445 79.940 20.174 1.00 63.33 A C ATOM 517 CG ARG A 106 26.657 80.816 19.724 1.00 74.03 A C ATOM 518 CD ARG A 106 26.603 81.494 18.313 1.00 80.90 A C ATOM 519 NE ARG A 106 26.088 82.878 18.300 1.00 82.99 A N ATOM 520 CZ ARG A 106 25.131 83.328 17.471 1.00 70.56 A C ATOM 521 NH1 ARG A 106 24.567 82.512 16.590 1.00 66.59 A N ATOM 522 NH2 ARG A 106 24.696 84.583 17.524 1.00 59.21 A N ATOM 523 C ARG A 106 24.883 77.580 19.359 1.00 61.94 A C ATOM 524 O ARG A 106 24.626 77.123 20.471 1.00 61.07 A O ATOM 525 N PHE A 107 25.224 76.826 18.322 1.00 54.56 A N ATOM 526 CA PHE A 107 25.719 75.480 18.493 1.00 54.78 A C ATOM 527 CB PHE A 107 26.266 74.968 17.156 1.00 52.25 A C ATOM 528 CG PHE A 107 26.527 73.502 17.135 1.00 51.95 A C ATOM 529 CD1 PHE A 107 26.105 72.710 18.180 1.00 45.55 A C ATOM 530 CD2 PHE A 107 27.167 72.909 16.059 1.00 52.01 A C ATOM 531 CE1 PHE A 107 26.325 71.351 18.176 1.00 50.09 A C ATOM 532 CE2 PHE A 107 27.390 71.542 16.048 1.00 47.98 A C ATOM 533 CZ PHE A 107 26.969 70.761 17.110 1.00 45.27 A C ATOM 534 C PHE A 107 26.819 75.554 19.557 1.00 59.06 A C ATOM 535 O PHE A 107 27.275 74.526 20.046 1.00 58.03 A O ATOM 536 N GLN A 108 27.216 76.790 19.893 1.00 63.09 A N ATOM 537 CA GLN A 108 28.173 77.160 20.958 1.00 60.52 A C ATOM 538 CB GLN A 108 29.050 75.992 21.401 1.00 55.63 A C ATOM 539 CG GLN A 108 30.384 75.979 20.699 1.00 50.74 A C ATOM 540 CD GLN A 108 31.216 74.775 21.038 1.00 56.80 A C ATOM 541 OE1 GLN A 108 30.734 73.822 21.655 1.00 62.20 A O ATOM 542 NE2 GLN A 108 32.479 74.802 20.630 1.00 50.38 A N ATOM 543 C GLN A 108 29.070 78.279 20.426 1.00 57.91 A C ATOM 544 O GLN A 108 29.054 78.555 19.226 1.00 57.93 A O ATOM 545 N THR A 109 29.854 78.912 21.300 1.00 53.71 A N ATOM 546 CA THR A 109 30.806 79.951 20.870 1.00 58.95 A C ATOM 547 CB THR A 109 31.276 80.831 22.047 1.00 62.47 A C ATOM 548 OG1 THR A 109 31.177 80.091 23.273 1.00 66.77 A O ATOM 549 CG2 THR A 109 30.433 82.098 22.135 1.00 51.24 A C ATOM 550 C THR A 109 32.041 79.404 20.140 1.00 54.70 A C ATOM 551 O THR A 109 32.784 78.590 20.687 1.00 50.69 A O ATOM 552 N PHE A 110 32.261 79.876 18.913 1.00 53.50 A N ATOM 553 CA PHE A 110 33.299 79.328 18.037 1.00 47.66 A C ATOM 554 CB PHE A 110 32.679 78.819 16.735 1.00 40.12 A C ATOM 555 CG PHE A 110 31.764 77.636 16.910 1.00 48.25 A C ATOM 556 CD1 PHE A 110 30.406 77.756 16.689 1.00 44.39 A C ATOM 557 CD2 PHE A 110 32.264 76.401 17.280 1.00 49.53 A C ATOM 558 CE1 PHE A 110 29.571 76.673 16.834 1.00 45.82 A C ATOM 559 CE2 PHE A 110 31.430 75.314 17.426 1.00 42.36 A C ATOM 560 CZ PHE A 110 30.084 75.451 17.205 1.00 45.97 A C ATOM 561 C PHE A 110 34.401 80.341 17.708 1.00 45.08 A C ATOM 562 O PHE A 110 34.219 81.546 17.858 1.00 49.08 A O ATOM 563 N GLU A 111 35.544 79.852 17.252 1.00 42.73 A N ATOM 564 CA GLU A 111 36.605 80.747 16.818 1.00 51.42 A C ATOM 565 CB GLU A 111 37.977 80.142 17.101 1.00 54.54 A C ATOM 566 CG GLU A 111 38.406 80.235 18.548 1.00 54.80 A C ATOM 567 CD GLU A 111 39.369 79.132 18.919 1.00 65.07 A C ATOM 568 OE1 GLU A 111 40.402 78.985 18.224 1.00 68.54 A O ATOM 569 OE2 GLU A 111 39.085 78.406 19.897 1.00 69.05 A O ATOM 570 C GLU A 111 36.494 81.071 15.338 1.00 53.82 A C ATOM 571 O GLU A 111 36.142 80.206 14.525 1.00 50.49 A O ATOM 572 N GLY A 112 36.778 82.330 15.007 1.00 47.86 A N ATOM 573 CA GLY A 112 36.965 82.752 13.633 1.00 43.93 A C ATOM 574 C GLY A 112 35.750 83.121 12.798 1.00 45.88 A C ATOM 575 O GLY A 112 34.634 83.272 13.291 1.00 40.08 A O ATOM 576 N ASP A 113 36.008 83.247 11.502 1.00 48.37 A N ATOM 577 CA ASP A 113 35.051 83.671 10.491 1.00 48.26 A C ATOM 578 CB ASP A 113 35.811 83.830 9.170 1.00 41.51 A C ATOM 579 CG ASP A 113 35.220 84.884 8.290 1.00 56.76 A C ATOM 580 OD1 ASP A 113 34.353 85.637 8.780 1.00 72.22 A O ATOM 581 OD2 ASP A 113 35.621 84.967 7.111 1.00 67.55 A O ATOM 582 C ASP A 113 33.884 82.690 10.283 1.00 51.11 A C ATOM 583 O ASP A 113 32.767 83.103 9.957 1.00 45.30 A O ATOM 584 N LEU A 114 34.164 81.399 10.466 1.00 45.57 A N ATOM 585 CA LEU A 114 33.242 80.300 10.145 1.00 45.38 A C ATOM 586 CB LEU A 114 31.840 80.506 10.730 1.00 36.97 A C ATOM 587 CG LEU A 114 31.800 80.702 12.254 1.00 42.71 A C ATOM 588 CD1 LEU A 114 30.479 80.256 12.815 1.00 31.50 A C ATOM 589 CD2 LEU A 114 32.934 79.956 12.944 1.00 43.31 A C ATOM 590 C LEU A 114 33.201 80.050 8.643 1.00 44.68 A C ATOM 591 O LEU A 114 32.243 79.493 8.106 1.00 46.16 A O ATOM 592 N LYS A 115 34.280 80.458 7.987 1.00 50.35 A N ATOM 593 CA LYS A 115 34.495 80.254 6.559 1.00 47.90 A C ATOM 594 CB LYS A 115 34.465 81.612 5.850 1.00 49.67 A C ATOM 595 CG LYS A 115 34.366 81.567 4.340 1.00 50.19 A C ATOM 596 CD LYS A 115 34.593 82.945 3.718 1.00 52.12 A C ATOM 597 CE LYS A 115 33.517 83.934 4.148 1.00 63.18 A C ATOM 598 NZ LYS A 115 33.513 85.166 3.300 1.00 67.09 A N ATOM 599 C LYS A 115 35.874 79.610 6.414 1.00 44.14 A C ATOM 600 O LYS A 115 36.776 79.899 7.201 1.00 44.44 A O ATOM 601 N TRP A 116 36.043 78.723 5.440 1.00 42.76 A N ATOM 602 CA TRP A 116 37.372 78.169 5.187 1.00 42.86 A C ATOM 603 CB TRP A 116 37.327 76.914 4.309 1.00 42.08 A C ATOM 604 CG TRP A 116 36.880 75.699 5.072 1.00 46.23 A C ATOM 605 CD2 TRP A 116 37.519 75.128 6.217 1.00 40.23 A C ATOM 606 CE2 TRP A 116 36.752 74.024 6.615 1.00 34.56 A C ATOM 607 CE3 TRP A 116 38.672 75.443 6.938 1.00 45.84 A C ATOM 608 CD1 TRP A 116 35.772 74.944 4.837 1.00 39.43 A C ATOM 609 NE1 TRP A 116 35.691 73.932 5.757 1.00 39.54 A N ATOM 610 CZ2 TRP A 116 37.096 73.230 7.698 1.00 40.54 A C ATOM 611 CZ3 TRP A 116 39.011 74.655 8.019 1.00 51.52 A C ATOM 612 CH2 TRP A 116 38.222 73.564 8.392 1.00 47.95 A C ATOM 613 C TRP A 116 38.200 79.229 4.521 1.00 46.35 A C ATOM 614 O TRP A 116 37.724 79.908 3.614 1.00 52.09 A O ATOM 615 N HIS A 117 39.439 79.388 4.972 1.00 48.59 A N ATOM 616 CA HIS A 117 40.289 80.412 4.386 1.00 51.18 A C ATOM 617 CB HIS A 117 40.743 81.436 5.429 1.00 47.66 A C ATOM 618 CG HIS A 117 39.714 82.486 5.711 1.00 50.85 A C ATOM 619 CD2 HIS A 117 39.347 83.585 5.009 1.00 52.70 A C ATOM 620 ND1 HIS A 117 38.895 82.450 6.820 1.00 58.35 A N ATOM 621 CE1 HIS A 117 38.080 83.488 6.798 1.00 55.30 A C ATOM 622 NE2 HIS A 117 38.332 84.193 5.710 1.00 60.46 A N ATOM 623 C HIS A 117 41.435 79.843 3.573 1.00 42.60 A C ATOM 624 O HIS A 117 42.403 80.529 3.284 1.00 44.06 A O ATOM 625 N HIS A 118 41.311 78.579 3.197 1.00 42.91 A N ATOM 626 CA HIS A 118 42.121 78.053 2.105 1.00 45.00 A C ATOM 627 CB HIS A 118 43.251 77.132 2.584 1.00 41.60 A C ATOM 628 CG HIS A 118 42.827 76.082 3.566 1.00 46.24 A C ATOM 629 CD2 HIS A 118 42.928 74.734 3.520 1.00 41.68 A C ATOM 630 ND1 HIS A 118 42.269 76.387 4.791 1.00 43.49 A N ATOM 631 CE1 HIS A 118 42.024 75.266 5.446 1.00 44.79 A C ATOM 632 NE2 HIS A 118 42.413 74.249 4.699 1.00 43.60 A N ATOM 633 C HIS A 118 41.247 77.375 1.063 1.00 44.65 A C ATOM 634 O HIS A 118 40.052 77.185 1.264 1.00 41.37 A O ATOM 635 N HIS A 119 41.853 77.032 −0.062 1.00 46.23 A N ATOM 636 CA HIS A 119 41.120 76.457 −1.171 1.00 46.67 A C ATOM 637 CB HIS A 119 41.836 76.777 −2.484 1.00 45.49 A C ATOM 638 CG HIS A 119 41.185 76.192 −3.698 1.00 57.97 A C ATOM 639 CD2 HIS A 119 41.632 75.283 −4.600 1.00 62.64 A C ATOM 640 ND1 HIS A 119 39.926 76.563 −4.122 1.00 56.61 A N ATOM 641 CE1 HIS A 119 39.617 75.896 −5.220 1.00 55.90 A C ATOM 642 NE2 HIS A 119 40.636 75.112 −5.533 1.00 57.65 A N ATOM 643 C HIS A 119 40.996 74.956 −0.973 1.00 47.84 A C ATOM 644 O HIS A 119 39.942 74.374 −1.231 1.00 50.64 A O ATOM 645 N ASN A 120 42.063 74.323 −0.499 1.00 46.57 A N ATOM 646 CA ASN A 120 42.055 72.869 −0.430 1.00 46.05 A C ATOM 647 CB ASN A 120 43.344 72.252 −0.918 1.00 44.36 A C ATOM 648 CG ASN A 120 43.275 70.763 −0.892 1.00 46.23 A C ATOM 649 OD1 ASN A 120 42.256 70.193 −1.269 1.00 44.96 A O ATOM 650 ND2 ASN A 120 44.331 70.114 −0.423 1.00 45.24 A N ATOM 651 C ASN A 120 41.758 72.311 0.937 1.00 49.66 A C ATOM 652 O ASN A 120 42.558 72.433 1.864 1.00 50.18 A O ATOM 653 N ILE A 121 40.610 71.657 1.031 1.00 45.74 A N ATOM 654 CA ILE A 121 40.099 71.191 2.297 1.00 45.02 A C ATOM 655 CB ILE A 121 38.581 71.506 2.395 1.00 46.43 A C ATOM 656 CG2 ILE A 121 38.049 71.292 3.806 1.00 37.70 A C ATOM 657 CG1 ILE A 121 38.309 72.944 1.922 1.00 35.20 A C ATOM 658 CD1 ILE A 121 39.030 74.000 2.707 1.00 33.05 A C ATOM 659 C ILE A 121 40.420 69.702 2.441 1.00 41.90 A C ATOM 660 O ILE A 121 40.025 68.888 1.606 1.00 40.05 A O ATOM 661 N THR A 122 41.179 69.360 3.479 1.00 43.18 A N ATOM 662 CA THR A 122 41.568 67.975 3.722 1.00 40.86 A C ATOM 663 CB THR A 122 42.943 67.869 4.405 1.00 35.11 A C ATOM 664 OG1 THR A 122 42.979 68.743 5.536 1.00 48.07 A O ATOM 665 CG2 THR A 122 44.049 68.250 3.461 1.00 33.19 A C ATOM 666 C THR A 122 40.548 67.334 4.636 1.00 40.12 A C ATOM 667 O THR A 122 39.945 68.016 5.454 1.00 43.82 A O ATOM 668 N TYR A 123 40.356 66.025 4.501 1.00 39.73 A N ATOM 669 CA TYR A 123 39.430 65.296 5.361 1.00 39.89 A C ATOM 670 CB TYR A 123 38.043 65.205 4.722 1.00 34.84 A C ATOM 671 CG TYR A 123 37.931 64.269 3.534 1.00 38.86 A C ATOM 672 CD1 TYR A 123 38.134 64.728 2.237 1.00 36.98 A C ATOM 673 CE1 TYR A 123 38.009 63.880 1.153 1.00 37.63 A C ATOM 674 CD2 TYR A 123 37.591 62.930 3.711 1.00 37.72 A C ATOM 675 CE2 TYR A 123 37.467 62.074 2.640 1.00 37.69 A C ATOM 676 CZ TYR A 123 37.678 62.550 1.361 1.00 45.19 A C ATOM 677 OH TYR A 123 37.558 61.690 0.291 1.00 40.14 A O ATOM 678 C TYR A 123 39.947 63.909 5.748 1.00 44.56 A C ATOM 679 O TYR A 123 40.570 63.210 4.941 1.00 45.12 A O ATOM 680 N TRP A 124 39.685 63.516 6.990 1.00 41.48 A N ATOM 681 CA TRP A 124 40.177 62.248 7.497 1.00 38.27 A C ATOM 682 CB TRP A 124 41.233 62.475 8.568 1.00 42.08 A C ATOM 683 CG TRP A 124 41.707 61.211 9.188 1.00 45.22 A C ATOM 684 CD2 TRP A 124 42.016 60.995 10.569 1.00 41.57 A C ATOM 685 CE2 TRP A 124 42.432 59.661 10.698 1.00 38.26 A C ATOM 686 CE3 TRP A 124 41.979 61.803 11.708 1.00 45.45 A C ATOM 687 CD1 TRP A 124 41.953 60.035 8.552 1.00 49.25 A C ATOM 688 NE1 TRP A 124 42.387 59.095 9.452 1.00 46.46 A N ATOM 689 CZ2 TRP A 124 42.812 59.114 11.917 1.00 42.80 A C ATOM 690 CZ3 TRP A 124 42.351 61.258 12.919 1.00 46.72 A C ATOM 691 CH2 TRP A 124 42.766 59.927 13.014 1.00 46.39 A C ATOM 692 C TRP A 124 39.070 61.402 8.069 1.00 41.98 A C ATOM 693 O TRP A 124 38.401 61.802 9.018 1.00 42.33 A O ATOM 694 N ILE A 125 38.887 60.222 7.488 1.00 48.44 A N ATOM 695 CA ILE A 125 37.915 59.255 7.981 1.00 39.99 A C ATOM 696 CB ILE A 125 37.565 58.238 6.888 1.00 41.05 A C ATOM 697 CG2 ILE A 125 36.412 57.348 7.330 1.00 43.17 A C ATOM 698 CG1 ILE A 125 37.262 58.969 5.571 1.00 39.02 A C ATOM 699 CD1 ILE A 125 36.780 58.068 4.447 1.00 37.03 A C ATOM 700 C ILE A 125 38.511 58.530 9.177 1.00 40.49 A C ATOM 701 O ILE A 125 39.200 57.530 9.016 1.00 42.25 A O ATOM 702 N GLN A 126 38.234 59.043 10.373 1.00 45.62 A N ATOM 703 CA GLN A 126 38.873 58.584 11.608 1.00 43.03 A C ATOM 704 CB GLN A 126 38.700 59.635 12.703 1.00 42.12 A C ATOM 705 CG GLN A 126 39.554 59.419 13.941 1.00 43.31 A C ATOM 706 CD GLN A 126 39.107 60.293 15.100 1.00 49.29 A C ATOM 707 OE1 GLN A 126 37.912 60.562 15.260 1.00 49.63 A O ATOM 708 NE2 GLN A 126 40.060 60.740 15.915 1.00 36.45 A N ATOM 709 C GLN A 126 38.388 57.220 12.116 1.00 48.28 A C ATOM 710 O GLN A 126 38.934 56.692 13.079 1.00 57.07 A O ATOM 711 N ASN A 127 37.370 56.656 11.478 1.00 44.99 A N ATOM 712 CA ASN A 127 36.925 55.303 11.804 1.00 48.02 A C ATOM 713 CB ASN A 127 36.533 55.191 13.276 1.00 45.59 A C ATOM 714 CG ASN A 127 35.253 55.923 13.589 1.00 49.16 A C ATOM 715 OD1 ASN A 127 34.777 56.723 12.789 1.00 46.12 A O ATOM 716 ND2 ASN A 127 34.683 55.651 14.758 1.00 50.93 A N ATOM 717 C ASN A 127 35.781 54.843 10.904 1.00 46.99 A C ATOM 718 O ASN A 127 35.571 55.409 9.834 1.00 46.92 A O ATOM 719 N TYR A 128 35.048 53.818 11.330 1.00 42.92 A N ATOM 720 CA TYR A 128 33.965 53.284 10.509 1.00 45.61 A C ATOM 721 CB TYR A 128 34.508 52.239 9.534 1.00 36.76 A C ATOM 722 CG TYR A 128 35.362 52.784 8.419 1.00 43.64 A C ATOM 723 CD1 TYR A 128 34.822 53.035 7.161 1.00 46.43 A C ATOM 724 CE1 TYR A 128 35.613 53.520 6.121 1.00 45.63 A C ATOM 725 CD2 TYR A 128 36.722 53.014 8.606 1.00 50.16 A C ATOM 726 CE2 TYR A 128 37.521 53.497 7.571 1.00 46.03 A C ATOM 727 CZ TYR A 128 36.962 53.745 6.332 1.00 42.81 A C ATOM 728 OH TYR A 128 37.752 54.229 5.309 1.00 35.57 A O ATOM 729 C TYR A 128 32.808 52.656 11.297 1.00 46.13 A C ATOM 730 O TYR A 128 33.008 52.111 12.382 1.00 49.50 A O ATOM 731 N SER A 129 31.601 52.739 10.735 1.00 40.60 A N ATOM 732 CA SER A 129 30.493 51.872 11.128 1.00 37.94 A C ATOM 733 CB SER A 129 29.157 52.513 10.748 1.00 38.93 A C ATOM 734 OG SER A 129 28.186 51.537 10.390 1.00 40.49 A O ATOM 735 C SER A 129 30.653 50.530 10.405 1.00 40.81 A C ATOM 736 O SER A 129 31.276 50.466 9.352 1.00 44.54 A O ATOM 737 N GLU A 130 30.103 49.459 10.966 1.00 40.43 A N ATOM 738 CA GLU A 130 30.216 48.136 10.349 1.00 43.33 A C ATOM 739 CB GLU A 130 30.562 47.064 11.396 1.00 41.96 A C ATOM 740 CG GLU A 130 31.942 47.224 12.040 1.00 50.00 A C ATOM 741 CD GLU A 130 33.099 46.872 11.096 1.00 55.87 A C ATOM 742 OE1 GLU A 130 32.875 46.139 10.109 1.00 54.14 A O ATOM 743 OE2 GLU A 130 34.240 47.320 11.348 1.00 56.47 A O ATOM 744 C GLU A 130 28.946 47.749 9.581 1.00 43.69 A C ATOM 745 O GLU A 130 28.829 46.629 9.081 1.00 33.63 A O ATOM 746 N ASP A 131 27.991 48.675 9.504 1.00 45.42 A N ATOM 747 CA ASP A 131 26.832 48.496 8.635 1.00 39.84 A C ATOM 748 CB ASP A 131 25.942 49.739 8.649 1.00 42.08 A C ATOM 749 CG ASP A 131 25.477 50.118 10.033 1.00 44.96 A C ATOM 750 OD1 ASP A 131 25.244 49.217 10.865 1.00 41.61 A O ATOM 751 OD2 ASP A 131 25.334 51.335 10.275 1.00 50.01 A O ATOM 752 C ASP A 131 27.252 48.257 7.187 1.00 41.77 A C ATOM 753 O ASP A 131 26.551 47.579 6.439 1.00 43.53 A O ATOM 754 N LEU A 132 28.389 48.831 6.790 1.00 40.67 A N ATOM 755 CA LEU A 132 28.741 48.929 5.379 1.00 35.56 A C ATOM 756 CB LEU A 132 28.396 50.327 4.868 1.00 30.94 A C ATOM 757 CG LEU A 132 26.916 50.667 4.717 1.00 44.13 A C ATOM 758 CD1 LEU A 132 26.676 52.183 4.642 1.00 39.18 A C ATOM 759 CD2 LEU A 132 26.358 49.960 3.492 1.00 47.17 A C ATOM 760 C LEU A 132 30.217 48.650 5.118 1.00 40.06 A C ATOM 761 O LEU A 132 31.069 48.964 5.948 1.00 49.88 A O ATOM 762 N PRO A 133 30.528 48.072 3.949 1.00 31.65 A N ATOM 763 CD PRO A 133 29.563 47.638 2.927 1.00 37.73 A C ATOM 764 CA PRO A 133 31.917 47.847 3.533 1.00 39.27 A C ATOM 765 CB PRO A 133 31.777 47.317 2.097 1.00 35.31 A C ATOM 766 CG PRO A 133 30.391 46.779 2.016 1.00 35.63 A C ATOM 767 C PRO A 133 32.716 49.148 3.514 1.00 42.95 A C ATOM 768 O PRO A 133 32.296 50.108 2.872 1.00 46.67 A O ATOM 769 N ARG A 134 33.858 49.170 4.190 1.00 40.02 A N ATOM 770 CA ARG A 134 34.685 50.368 4.248 1.00 40.97 A C ATOM 771 CB ARG A 134 36.033 50.052 4.887 1.00 42.84 A C ATOM 772 CG ARG A 134 35.937 49.671 6.349 1.00 52.35 A C ATOM 773 CD ARG A 134 37.262 49.885 7.038 1.00 52.29 A C ATOM 774 NE ARG A 134 37.275 49.358 8.395 1.00 54.19 A N ATOM 775 CZ ARG A 134 38.368 49.304 9.148 1.00 60.82 A C ATOM 776 NH1 ARG A 134 39.526 49.742 8.664 1.00 54.36 A N ATOM 777 NH2 ARG A 134 38.308 48.814 10.380 1.00 65.72 A N ATOM 778 C ARG A 134 34.898 51.034 2.890 1.00 40.42 A C ATOM 779 O ARG A 134 35.014 52.252 2.802 1.00 44.90 A O ATOM 780 N ALA A 135 34.963 50.244 1.829 1.00 40.83 A N ATOM 781 CA ALA A 135 35.088 50.826 0.503 1.00 45.18 A C ATOM 782 CB ALA A 135 35.290 49.749 −0.543 1.00 40.69 A C ATOM 783 C ALA A 135 33.841 51.660 0.200 1.00 49.47 A C ATOM 784 O ALA A 135 33.942 52.805 −0.240 1.00 49.60 A O ATOM 785 N VAL A 136 32.667 51.093 0.462 1.00 42.93 A N ATOM 786 CA VAL A 136 31.419 51.795 0.177 1.00 44.82 A C ATOM 787 CB VAL A 136 30.214 50.834 0.179 1.00 45.28 A C ATOM 788 CG1 VAL A 136 28.904 51.607 0.168 1.00 43.53 A C ATOM 789 CG2 VAL A 136 30.292 49.913 −1.020 1.00 41.86 A C ATOM 790 C VAL A 136 31.151 53.011 1.075 1.00 38.60 A C ATOM 791 O VAL A 136 30.336 53.857 0.738 1.00 36.43 A O ATOM 792 N ILE A 137 31.836 53.102 2.209 1.00 41.57 A N ATOM 793 CA ILE A 137 31.736 54.292 3.052 1.00 40.82 A C ATOM 794 CB ILE A 137 32.122 54.006 4.529 1.00 41.43 A C ATOM 795 CG2 ILE A 137 32.339 55.302 5.291 1.00 35.32 A C ATOM 796 CG1 ILE A 137 31.035 53.179 5.226 1.00 40.62 A C ATOM 797 CD1 ILE A 137 31.238 53.011 6.733 1.00 34.08 A C ATOM 798 C ILE A 137 32.663 55.357 2.475 1.00 42.18 A C ATOM 799 O ILE A 137 32.322 56.541 2.404 1.00 41.58 A O ATOM 800 N ASP A 138 33.836 54.909 2.045 1.00 40.62 A N ATOM 801 CA ASP A 138 34.812 55.768 1.397 1.00 38.08 A C ATOM 802 CB ASP A 138 36.018 54.932 0.966 1.00 37.43 A C ATOM 803 CG ASP A 138 36.833 54.422 2.144 1.00 43.62 A C ATOM 804 OD1 ASP A 138 36.385 54.574 3.301 1.00 37.62 A O ATOM 805 OD2 ASP A 138 37.931 53.870 1.906 1.00 43.96 A O ATOM 806 C ASP A 138 34.228 56.481 0.177 1.00 40.95 A C ATOM 807 O ASP A 138 34.522 57.655 −0.076 1.00 42.39 A O ATOM 808 N ASP A 139 33.412 55.761 −0.586 1.00 37.43 A N ATOM 809 CA ASP A 139 32.832 56.301 −1.808 1.00 39.64 A C ATOM 810 CB ASP A 139 32.382 55.169 −2.725 1.00 40.52 A C ATOM 811 CG ASP A 139 31.724 55.674 −3.992 1.00 41.98 A C ATOM 812 OD1 ASP A 139 32.451 56.114 −4.914 1.00 45.33 A O ATOM 813 OD2 ASP A 139 30.480 55.617 −4.071 1.00 33.52 A O ATOM 814 C ASP A 139 31.650 57.216 −1.522 1.00 43.20 A C ATOM 815 O ASP A 139 31.386 58.150 −2.277 1.00 42.92 A O ATOM 816 N ALA A 140 30.925 56.935 −0.444 1.00 40.69 A N ATOM 817 CA ALA A 140 29.761 57.741 −0.089 1.00 43.22 A C ATOM 818 CB ALA A 140 28.922 57.048 0.982 1.00 38.02 A C ATOM 819 C ALA A 140 30.177 59.140 0.368 1.00 43.38 A C ATOM 820 O ALA A 140 29.471 60.115 0.136 1.00 41.16 A O ATOM 821 N PHE A 141 31.325 59.248 1.021 1.00 45.71 A N ATOM 822 CA PHE A 141 31.790 60.564 1.433 1.00 46.15 A C ATOM 823 CB PHE A 141 32.862 60.467 2.520 1.00 43.69 A C ATOM 824 CG PHE A 141 32.351 59.947 3.839 1.00 41.91 A C ATOM 825 CD1 PHE A 141 31.160 60.410 4.374 1.00 47.14 A C ATOM 826 CD2 PHE A 141 33.077 59.013 4.562 1.00 44.69 A C ATOM 827 CE1 PHE A 141 30.694 59.935 5.608 1.00 39.29 A C ATOM 828 CE2 PHE A 141 32.617 58.541 5.788 1.00 38.94 A C ATOM 829 CZ PHE A 141 31.432 59.005 6.309 1.00 31.58 A C ATOM 830 C PHE A 141 32.307 61.325 0.218 1.00 42.72 A C ATOM 831 O PHE A 141 31.998 62.509 0.036 1.00 41.23 A O ATOM 832 N ALA A 142 33.072 60.628 −0.620 1.00 42.88 A N ATOM 833 CA ALA A 142 33.656 61.217 −1.830 1.00 41.56 A C ATOM 834 CB ALA A 142 34.419 60.160 −2.620 1.00 38.11 A C ATOM 835 C ALA A 142 32.593 61.865 −2.707 1.00 36.22 A C ATOM 836 O ALA A 142 32.711 63.031 −3.091 1.00 33.19 A O ATOM 837 N ARG A 143 31.557 61.092 −3.013 1.00 38.42 A N ATOM 838 CA ARG A 143 30.433 61.562 −3.809 1.00 35.08 A C ATOM 839 CB ARG A 143 29.424 60.441 −3.997 1.00 35.80 A C ATOM 840 CG ARG A 143 29.831 59.351 −4.964 1.00 30.32 A C ATOM 841 CD ARG A 143 29.156 58.058 −4.546 1.00 40.76 A C ATOM 842 NE ARG A 143 27.710 58.232 −4.379 1.00 45.34 A N ATOM 843 CZ ARG A 143 26.940 57.502 −3.572 1.00 43.79 A C ATOM 844 NH1 ARG A 143 27.462 56.542 −2.815 1.00 40.55 A N ATOM 845 NH2 ARG A 143 25.640 57.746 −3.512 1.00 45.12 A N ATOM 846 C ARG A 143 29.754 62.732 −3.117 1.00 35.96 A C ATOM 847 O ARG A 143 29.196 63.610 −3.769 1.00 35.25 A O ATOM 848 N ALA A 144 29.809 62.733 −1.789 1.00 37.43 A N ATOM 849 CA ALA A 144 29.154 63.763 −0.999 1.00 38.17 A C ATOM 850 CB ALA A 144 29.075 63.344 0.458 1.00 37.91 A C ATOM 851 C ALA A 144 29.899 65.082 −1.144 1.00 40.95 A C ATOM 852 O ALA A 144 29.282 66.151 −1.265 1.00 36.68 A O ATOM 853 N PHE A 145 31.230 64.994 −1.129 1.00 42.51 A N ATOM 854 CA PHE A 145 32.092 66.142 −1.388 1.00 32.53 A C ATOM 855 CB PHE A 145 33.539 65.829 −1.029 1.00 35.94 A C ATOM 856 CG PHE A 145 33.834 65.883 0.443 1.00 37.74 A C ATOM 857 CD1 PHE A 145 33.538 67.018 1.185 1.00 35.05 A C ATOM 858 CD2 PHE A 145 34.440 64.803 1.080 1.00 33.17 A C ATOM 859 CE1 PHE A 145 33.831 67.069 2.541 1.00 37.52 A C ATOM 860 CE2 PHE A 145 34.730 64.841 2.429 1.00 29.05 A C ATOM 861 CZ PHE A 145 34.431 65.976 3.163 1.00 36.76 A C ATOM 862 C PHE A 145 32.021 66.498 −2.858 1.00 31.13 A C ATOM 863 O PHE A 145 32.093 67.665 −3.231 1.00 38.12 A O ATOM 864 N ALA A 146 31.881 65.487 −3.698 1.00 29.39 A N ATOM 865 CA ALA A 146 31.830 65.727 −5.130 1.00 32.09 A C ATOM 866 CB ALA A 146 31.694 64.419 −5.886 1.00 25.89 A C ATOM 867 C ALA A 146 30.701 66.694 −5.492 1.00 33.03 A C ATOM 868 O ALA A 146 30.708 67.283 −6.569 1.00 39.49 A O ATOM 869 N LEU A 147 29.735 66.857 −4.595 1.00 31.00 A N ATOM 870 CA LEU A 147 28.639 67.805 −4.824 1.00 40.30 A C ATOM 871 CB LEU A 147 27.421 67.467 −3.959 1.00 33.31 A C ATOM 872 CG LEU A 147 26.682 66.141 −4.094 1.00 36.71 A C ATOM 873 CD1 LEU A 147 25.711 66.008 −2.925 1.00 37.37 A C ATOM 874 CD2 LEU A 147 25.950 66.036 −5.418 1.00 26.22 A C ATOM 875 C LEU A 147 29.038 69.257 −4.541 1.00 38.47 A C ATOM 876 O LEU A 147 28.702 70.161 −5.295 1.00 35.87 A O ATOM 877 N TRP A 148 29.725 69.476 −3.430 1.00 36.50 A N ATOM 878 CA TRP A 148 30.039 70.819 −3.010 1.00 35.94 A C ATOM 879 CB TRP A 148 30.357 70.848 −1.514 1.00 39.58 A C ATOM 880 CG TRP A 148 29.176 70.543 −0.590 1.00 44.37 A C ATOM 881 CD2 TRP A 148 27.969 71.309 −0.444 1.00 38.36 A C ATOM 882 CE2 TRP A 148 27.174 70.661 0.521 1.00 41.11 A C ATOM 883 CE3 TRP A 148 27.481 72.476 −1.037 1.00 36.75 A C ATOM 884 CD1 TRP A 148 29.066 69.497 0.286 1.00 38.34 A C ATOM 885 NE1 TRP A 148 27.864 69.556 0.950 1.00 36.28 A N ATOM 886 CZ2 TRP A 148 25.924 71.147 0.908 1.00 37.91 A C ATOM 887 CZ3 TRP A 148 26.231 72.946 −0.658 1.00 27.33 A C ATOM 888 CH2 TRP A 148 25.477 72.291 0.305 1.00 27.25 A C ATOM 889 C TRP A 148 31.218 71.360 −3.812 1.00 45.39 A C ATOM 890 O TRP A 148 31.389 72.570 −3.951 1.00 47.98 A O ATOM 891 N SER A 149 32.042 70.468 −4.342 1.00 39.84 A N ATOM 892 CA SER A 149 33.196 70.922 −5.097 1.00 39.66 A C ATOM 893 CB SER A 149 34.214 69.797 −5.261 1.00 35.74 A C ATOM 894 OG SER A 149 33.849 68.947 −6.328 1.00 38.64 A O ATOM 895 C SER A 149 32.790 71.496 −6.461 1.00 41.43 A C ATOM 896 O SER A 149 33.298 72.535 −6.877 1.00 44.16 A O ATOM 897 N ALA A 150 31.869 70.831 −7.149 1.00 34.70 A N ATOM 898 CA ALA A 150 31.451 71.284 −8.469 1.00 38.94 A C ATOM 899 CB ALA A 150 30.457 70.311 −9.076 1.00 35.49 A C ATOM 900 C ALA A 150 30.876 72.703 −8.459 1.00 41.16 A C ATOM 901 O ALA A 150 30.783 73.356 −9.503 1.00 41.26 A O ATOM 902 N VAL A 151 30.504 73.183 −7.279 1.00 42.06 A N ATOM 903 CA VAL A 151 29.802 74.459 −7.163 1.00 41.64 A C ATOM 904 CB VAL A 151 28.369 74.248 −6.673 1.00 37.55 A C ATOM 905 CG1 VAL A 151 27.622 73.366 −7.645 1.00 31.20 A C ATOM 906 CG2 VAL A 151 28.377 73.620 −5.285 1.00 41.04 A C ATOM 907 C VAL A 151 30.519 75.451 −6.245 1.00 42.34 A C ATOM 908 O VAL A 151 30.004 76.525 −5.955 1.00 42.81 A O ATOM 909 N THR A 152 31.713 75.081 −5.798 1.00 38.65 A N ATOM 910 CA THR A 152 32.527 75.962 −4.984 1.00 41.50 A C ATOM 911 CB THR A 152 32.632 75.469 −3.530 1.00 47.07 A C ATOM 912 OG1 THR A 152 33.112 74.119 −3.521 1.00 47.18 A O ATOM 913 CG2 THR A 152 31.286 75.537 −2.824 1.00 45.18 A C ATOM 914 C THR A 152 33.936 75.991 −5.543 1.00 47.37 A C ATOM 915 O THR A 152 34.374 75.038 −6.182 1.00 44.00 A O ATOM 916 N PRO A 153 34.644 77.104 −5.326 1.00 48.44 A N ATOM 917 CD PRO A 153 34.103 78.454 −5.096 1.00 43.82 A C ATOM 918 CA PRO A 153 36.090 77.136 −5.536 1.00 47.51 A C ATOM 919 CB PRO A 153 36.413 78.627 −5.411 1.00 47.79 A C ATOM 920 CG PRO A 153 35.281 79.168 −4.550 1.00 45.42 A C ATOM 921 C PRO A 153 36.771 76.374 −4.407 1.00 47.92 A C ATOM 922 O PRO A 153 37.545 76.968 −3.662 1.00 54.80 A O ATOM 923 N LEU A 154 36.466 75.088 −4.265 1.00 48.13 A N ATOM 924 CA LEU A 154 37.070 74.261 −3.224 1.00 44.42 A C ATOM 925 CB LEU A 154 36.127 74.137 −2.025 1.00 45.56 A C ATOM 926 CG LEU A 154 35.774 75.362 −1.172 1.00 46.87 A C ATOM 927 CD1 LEU A 154 34.857 74.954 −0.035 1.00 41.76 A C ATOM 928 CD2 LEU A 154 37.009 76.035 −0.621 1.00 40.70 A C ATOM 929 C LEU A 154 37.384 72.866 −3.743 1.00 42.40 A C ATOM 930 O LEU A 154 36.636 72.317 −4.552 1.00 43.63 A O ATOM 931 N THR A 155 38.485 72.288 −3.272 1.00 41.09 A N ATOM 932 CA THR A 155 38.779 70.880 −3.534 1.00 35.89 A C ATOM 933 CB THR A 155 40.135 70.676 −4.236 1.00 37.39 A C ATOM 934 OG1 THR A 155 41.108 71.559 −3.664 1.00 47.03 A O ATOM 935 CG2 THR A 155 40.009 70.947 −5.720 1.00 39.81 A C ATOM 936 C THR A 155 38.800 70.084 −2.240 1.00 39.71 A C ATOM 937 O THR A 155 39.094 70.615 −1.169 1.00 41.35 A O ATOM 938 N PHE A 156 38.505 68.797 −2.342 1.00 37.31 A N ATOM 939 CA PHE A 156 38.477 67.959 −1.162 1.00 39.59 A C ATOM 940 CB PHE A 156 37.042 67.515 −0.853 1.00 37.81 A C ATOM 941 CG PHE A 156 36.093 68.664 −0.701 1.00 38.38 A C ATOM 942 CD1 PHE A 156 35.306 69.072 −1.760 1.00 37.70 A C ATOM 943 CD2 PHE A 156 36.021 69.367 0.490 1.00 38.34 A C ATOM 944 CE1 PHE A 156 34.457 70.137 −1.632 1.00 32.30 A C ATOM 945 CE2 PHE A 156 35.169 70.435 0.618 1.00 37.95 A C ATOM 946 CZ PHE A 156 34.388 70.818 −0.448 1.00 34.11 A C ATOM 947 C PHE A 156 39.435 66.789 −1.308 1.00 39.55 A C ATOM 948 O PHE A 156 39.335 65.977 −2.226 1.00 39.02 A O ATOM 949 N THR A 157 40.376 66.723 −0.386 1.00 37.75 A N ATOM 950 CA THR A 157 41.458 65.771 −0.474 1.00 40.55 A C ATOM 951 CB THR A 157 42.796 66.513 −0.666 1.00 43.34 A C ATOM 952 OG1 THR A 157 42.926 66.909 −2.036 1.00 41.00 A O ATOM 953 CG2 THR A 157 43.947 65.631 −0.293 1.00 40.02 A C ATOM 954 C THR A 157 41.503 64.939 0.796 1.00 43.28 A C ATOM 955 O THR A 157 41.546 65.482 1.902 1.00 37.87 A O ATOM 956 N ARG A 158 41.483 63.619 0.629 1.00 45.97 A N ATOM 957 CA ARG A 158 41.479 62.698 1.763 1.00 48.13 A C ATOM 958 CB ARG A 158 40.867 61.358 1.362 1.00 41.11 A C ATOM 959 CG ARG A 158 41.072 60.287 2.395 1.00 36.93 A C ATOM 960 CD ARG A 158 40.627 58.948 1.872 1.00 38.87 A C ATOM 961 NE ARG A 158 40.686 57.931 2.914 1.00 39.75 A N ATOM 962 CZ ARG A 158 40.205 56.701 2.776 1.00 41.47 A C ATOM 963 NH1 ARG A 158 39.619 56.340 1.638 1.00 32.69 A N ATOM 964 NH2 ARG A 158 40.304 55.837 3.779 1.00 36.91 A N ATOM 965 C ARG A 158 42.879 62.474 2.336 1.00 45.23 A C ATOM 966 O ARG A 158 43.847 62.342 1.591 1.00 42.73 A O ATOM 967 N VAL A 159 42.973 62.438 3.662 1.00 47.17 A N ATOM 968 CA VAL A 159 44.249 62.238 4.347 1.00 51.53 A C ATOM 969 CB VAL A 159 44.802 63.561 4.903 1.00 44.96 A C ATOM 970 CG1 VAL A 159 44.743 64.642 3.836 1.00 41.71 A C ATOM 971 CG2 VAL A 159 44.023 63.976 6.132 1.00 41.47 A C ATOM 972 C VAL A 159 44.109 61.230 5.495 1.00 57.18 A C ATOM 973 O VAL A 159 43.022 60.673 5.720 1.00 53.41 A O ATOM 974 N TYR A 160 45.199 61.003 6.228 1.00 51.13 A N ATOM 975 CA TYR A 160 45.196 59.957 7.248 1.00 46.79 A C ATOM 976 CB TYR A 160 45.963 58.737 6.737 1.00 40.00 A C ATOM 977 CG TYR A 160 45.255 58.088 5.573 1.00 45.10 A C ATOM 978 CD1 TYR A 160 45.457 58.528 4.265 1.00 49.58 A C ATOM 979 CE1 TYR A 160 44.780 57.936 3.198 1.00 41.76 A C ATOM 980 CD2 TYR A 160 44.351 57.060 5.781 1.00 44.65 A C ATOM 981 CE2 TYR A 160 43.679 56.468 4.729 1.00 42.75 A C ATOM 982 CZ TYR A 160 43.891 56.908 3.446 1.00 38.36 A C ATOM 983 OH TYR A 160 43.202 56.301 2.424 1.00 42.28 A O ATOM 984 C TYR A 160 45.699 60.414 8.613 1.00 49.65 A C ATOM 985 O TYR A 160 46.354 59.659 9.334 1.00 50.66 A O ATOM 986 N SER A 161 45.356 61.645 8.975 1.00 46.05 A N ATOM 987 CA SER A 161 45.850 62.251 10.203 1.00 48.54 A C ATOM 988 CB SER A 161 47.191 62.947 9.944 1.00 55.90 A C ATOM 989 OG SER A 161 47.049 64.009 9.006 1.00 60.58 A O ATOM 990 C SER A 161 44.853 63.257 10.777 1.00 53.00 A C ATOM 991 O SER A 161 43.921 63.685 10.097 1.00 48.39 A O ATOM 222 N ARG A 162 45.065 63.636 12.032 1.00 50.80 A N ATOM 993 CA ARG A 162 44.215 64.609 12.698 1.00 52.52 A C ATOM 994 CB ARG A 162 44.490 64.588 14.202 1.00 66.58 A C ATOM 995 CG ARG A 162 44.693 65.953 14.843 1.00 68.63 A C ATOM 996 CD ARG A 162 45.694 65.838 15.979 1.00 68.43 A C ATOM 997 NE ARG A 162 46.759 64.900 15.632 1.00 72.12 A N ATOM 998 CZ ARG A 162 47.586 64.341 16.509 1.00 80.60 A C ATOM 999 NH1 ARG A 162 47.476 64.621 17.804 1.00 73.93 A N ATOM 1000 NH2 ARG A 162 48.522 63.496 16.090 1.00 68.46 A N ATOM 1001 C ARG A 162 44.437 66.003 12.144 1.00 54.65 A C ATOM 1002 O ARG A 162 43.697 66.930 12.452 1.00 57.84 A O ATOM 1003 N ASP A 163 45.456 66.149 11.309 1.00 65.80 A N ATOM 1004 CA ASP A 163 45.811 67.456 10.767 1.00 66.90 A C ATOM 1005 CB ASP A 163 47.256 67.442 10.267 1.00 69.55 A C ATOM 1006 CG ASP A 163 47.919 68.799 10.378 1.00 77.87 A C ATOM 1007 OD1 ASP A 163 47.834 69.406 11.469 1.00 72.47 A O ATOM 1008 OD2 ASP A 163 48.524 69.252 9.379 1.00 76.64 A O ATOM 1009 C ASP A 163 44.870 67.923 9.645 1.00 59.97 A C ATOM 1010 O ASP A 163 45.092 68.970 9.033 1.00 54.83 A O ATOM 1011 N ALA A 164 43.820 67.152 9.382 1.00 52.59 A N ATOM 1012 CA ALA A 164 42.890 67.497 8.315 1.00 46.75 A C ATOM 1013 CB ALA A 164 42.177 66.262 7.823 1.00 45.52 A C ATOM 1014 C ALA A 164 41.883 68.554 8.765 1.00 50.10 A C ATOM 1015 O ALA A 164 41.469 68.580 9.924 1.00 45.67 A O ATOM 1016 N ASP A 165 41.505 69.431 7.840 1.00 49.12 A N ATOM 1017 CA ASP A 165 40.475 70.430 8.098 1.00 46.81 A C ATOM 1018 CB ASP A 165 40.153 71.212 6.823 1.00 48.31 A C ATOM 1019 CG ASP A 165 41.389 71.683 6.092 1.00 49.96 A C ATOM 1020 OD1 ASP A 165 42.307 72.202 6.761 1.00 57.10 A O ATOM 1021 OD2 ASP A 165 41.434 71.551 4.848 1.00 40.05 A O ATOM 1022 C ASP A 165 39.193 69.765 8.584 1.00 49.76 A C ATOM 1023 O ASP A 165 38.471 70.320 9.416 1.00 51.93 A O ATOM 1024 N ILE A 166 38.900 68.582 8.045 1.00 46.34 A N ATOM 1025 CA ILE A 166 37.658 67.882 8.369 1.00 47.71 A C ATOM 1026 CB ILE A 166 36.702 67.839 7.160 1.00 42.91 A C ATOM 1027 CG2 ILE A 166 35.365 67.232 7.559 1.00 44.34 A C ATOM 1028 CG1 ILE A 166 36.495 69.234 6.583 1.00 42.84 A C ATOM 1029 CD1 ILE A 166 35.255 69.345 5.710 1.00 43.27 A C ATOM 1030 C ILE A 166 37.866 66.447 8.862 1.00 43.66 A C ATOM 1031 O ILE A 166 38.131 65.547 8.070 1.00 38.28 A O ATOM 1032 N VAL A 167 37.730 66.242 10.171 1.00 43.55 A N ATOM 1033 CA VAL A 167 37.807 64.902 10.753 1.00 43.31 A C ATOM 1034 CB VAL A 167 38.393 64.932 12.167 1.00 49.52 A C ATOM 1035 CG1 VAL A 167 38.624 63.514 12.670 1.00 48.56 A C ATOM 1036 CG2 VAL A 167 39.684 65.733 12.184 1.00 44.69 A C ATOM 1037 C VAL A 167 36.432 64.233 10.805 1.00 40.56 A C ATOM 1038 O VAL A 167 35.483 64.767 11.370 1.00 43.26 A O ATOM 1039 N ILE A 168 36.338 63.057 10.206 1.00 39.85 A N ATOM 1040 CA ILE A 168 35.070 62.362 10.062 1.00 39.18 A C ATOM 1041 CB ILE A 168 34.849 61.946 8.588 1.00 36.61 A C ATOM 1042 CG2 ILE A 168 33.826 60.833 8.460 1.00 35.97 A C ATOM 1043 CG1 ILE A 168 34.427 63.161 7.762 1.00 39.08 A C ATOM 1044 CD1 ILE A 168 34.124 62.833 6.313 1.00 44.23 A C ATOM 1045 C ILE A 168 35.024 61.159 10.999 1.00 38.30 A C ATOM 1046 O ILE A 168 35.902 60.299 10.972 1.00 36.56 A O ATOM 1047 N GLN A 169 33.994 61.108 11.833 1.00 41.28 A N ATOM 1048 CA GLN A 169 33.959 60.134 12.919 1.00 45.36 A C ATOM 1049 CB GLN A 169 34.496 60.779 14.199 1.00 49.64 A C ATOM 1050 CG GLN A 169 34.184 60.038 15.479 1.00 47.23 A C ATOM 1051 CD GLN A 169 34.877 60.675 16.666 1.00 50.98 A C ATOM 1052 OE1 GLN A 169 35.772 61.505 16.497 1.00 50.74 A O ATOM 1053 NE2 GLN A 169 34.471 60.292 17.871 1.00 52.60 A N ATOM 1054 C GLN A 169 32.575 59.554 13.158 1.00 37.52 A C ATOM 1055 O GLN A 169 31.577 60.252 13.065 1.00 44.21 A O ATOM 1056 N PHE A 170 32.529 58.260 13.438 1.00 38.70 A N ATOM 1057 CA PHE A 170 31.301 57.604 13.854 1.00 41.18 A C ATOM 1058 CB PHE A 170 31.206 56.210 13.232 1.00 39.26 A C ATOM 1059 CG PHE A 170 31.041 56.216 11.730 1.00 38.08 A C ATOM 1060 CD1 PHE A 170 32.117 56.497 10.896 1.00 41.99 A C ATOM 1061 CD2 PHE A 170 29.816 55.921 11.151 1.00 35.22 A C ATOM 1062 CE1 PHE A 170 31.974 56.498 9.508 1.00 38.90 A C ATOM 1063 CE2 PHE A 170 29.667 55.918 9.757 1.00 43.81 A C ATOM 1064 CZ PHE A 170 30.749 56.210 8.939 1.00 37.30 A C ATOM 1065 C PHE A 170 31.265 57.521 15.391 1.00 42.97 A C ATOM 1066 O PHE A 170 32.291 57.332 16.041 1.00 38.89 A O ATOM 1067 N GLY A 171 30.089 57.676 15.978 1.00 39.22 A N ATOM 1068 CA GLY A 171 30.006 57.652 17.422 1.00 43.04 A C ATOM 1069 C GLY A 171 28.637 57.277 17.930 1.00 46.38 A C ATOM 1070 O GLY A 171 27.653 57.360 17.195 1.00 43.66 A O ATOM 1071 N VAL A 172 28.583 56.838 19.185 1.00 44.13 A N ATOM 1072 CA VAL A 172 27.317 56.613 19.866 1.00 40.95 A C ATOM 1073 CB VAL A 172 27.027 55.109 20.107 1.00 40.62 A C ATOM 1074 CG1 VAL A 172 26.959 54.354 18.789 1.00 41.88 A C ATOM 1075 CG2 VAL A 172 28.076 54.503 21.011 1.00 47.38 A C ATOM 1076 C VAL A 172 27.349 57.356 21.192 1.00 42.87 A C ATOM 1077 O VAL A 172 28.384 57.415 21.852 1.00 42.41 A O ATOM 1078 N ALA A 173 26.223 57.943 21.570 1.00 45.71 A N ATOM 1079 CA ALA A 173 26.135 58.615 22.856 1.00 48.78 A C ATOM 1080 CB ALA A 173 26.176 57.598 23.978 1.00 46.11 A C ATOM 1081 C ALA A 173 27.269 59.622 23.003 1.00 48.28 A C ATOM 1082 O ALA A 173 27.528 60.400 22.089 1.00 49.88 A O ATOM 1083 N GLU A 174 27.943 59.613 24.150 1.00 49.13 A N ATOM 1084 CA GLU A 174 29.070 60.522 24.362 1.00 58.08 A C ATOM 1085 CB GLU A 174 29.282 60.808 25.852 1.00 52.66 A C ATOM 1086 CG GLU A 174 30.548 61.610 26.154 1.00 58.78 A C ATOM 1087 CD GLU A 174 30.548 63.002 25.534 1.00 59.48 A C ATOM 1088 OE1 GLU A 174 29.465 63.499 25.151 1.00 55.88 A O ATOM 1089 OE2 GLU A 174 31.641 63.603 25.435 1.00 60.46 A O ATOM 1090 C GLU A 174 30.358 59.995 23.721 1.00 53.01 A C ATOM 1091 O GLU A 174 30.834 58.904 24.045 1.00 51.94 A O ATOM 1092 N HIS A 175 30.919 60.787 22.819 1.00 50.40 A N ATOM 1093 CA HIS A 175 32.053 60.349 22.006 1.00 50.47 A C ATOM 1094 CB HIS A 175 31.581 60.067 20.581 1.00 48.12 A C ATOM 1095 CG HIS A 175 30.635 61.100 20.059 1.00 47.64 A C ATOM 1096 CD2 HIS A 175 30.852 62.243 19.366 1.00 48.22 A C ATOM 1097 ND1 HIS A 175 29.277 61.034 20.272 1.00 45.89 A N ATOM 1098 CE1 HIS A 175 28.695 62.082 19.717 1.00 45.76 A C ATOM 1099 NE2 HIS A 175 29.627 62.829 19.159 1.00 39.11 A N ATOM 1100 C HIS A 175 33.192 61.368 21.978 1.00 45.82 A C ATOM 1101 O HIS A 175 33.998 61.377 21.050 1.00 47.84 A O ATOM 1102 N GLY A 176 33.238 62.237 22.983 1.00 49.29 A N ATOM 1103 CA GLY A 176 34.398 63.077 23.204 1.00 43.18 A C ATOM 1104 C GLY A 176 34.253 64.565 22.945 1.00 46.89 A C ATOM 1105 O GLY A 176 35.266 65.263 22.790 1.00 37.40 A O ATOM 1106 N ASP A 177 33.023 65.073 22.909 1.00 46.04 A N ATOM 1107 CA ASP A 177 32.844 66.487 22.563 1.00 46.91 A C ATOM 1108 CB ASP A 177 32.640 66.660 21.053 1.00 43.92 A C ATOM 1109 CG ASP A 177 31.303 66.121 20.572 1.00 44.98 A C ATOM 1110 OD1 ASP A 177 30.543 65.547 21.382 1.00 43.91 A O ATOM 1111 OD2 ASP A 177 31.016 66.279 19.368 1.00 40.34 A O ATOM 1112 C ASP A 177 31.743 67.228 23.309 1.00 49.54 A C ATOM 1113 O ASP A 177 31.454 68.377 22.986 1.00 59.49 A O ATOM 1114 N GLY A 178 31.129 66.581 24.293 1.00 50.91 A N ATOM 1115 CA GLY A 178 30.082 67.220 25.070 1.00 51.44 A C ATOM 1116 C GLY A 178 28.811 67.524 24.297 1.00 48.15 A C ATOM 1117 O GLY A 178 28.058 68.435 24.645 1.00 53.49 A O ATOM 1118 N TYR A 179 28.588 66.774 23.226 1.00 49.83 A N ATOM 1119 CA TYR A 179 27.300 66.750 22.551 1.00 48.79 A C ATOM 1120 CB TYR A 179 27.331 67.557 21.259 1.00 43.85 A C ATOM 1121 CG TYR A 179 27.400 69.049 21.467 1.00 45.92 A C ATOM 1122 CD1 TYR A 179 28.611 69.676 21.734 1.00 51.48 A C ATOM 1123 CE1 TYR A 179 28.681 71.043 21.917 1.00 50.00 A C ATOM 1124 CD2 TYR A 179 26.261 69.836 21.376 1.00 43.94 A C ATOM 1125 CE2 TYR A 179 26.321 71.201 21.553 1.00 41.37 A C ATOM 1126 CZ TYR A 179 27.532 71.797 21.826 1.00 45.57 A C ATOM 1127 OH TYR A 179 27.602 73.155 22.007 1.00 50.59 A O ATOM 1128 C TYR A 179 26.987 65.293 22.255 1.00 51.91 A C ATOM 1129 O TYR A 179 27.276 64.793 21.170 1.00 51.33 A O ATOM 1130 N PRO A 180 26.410 64.597 23.237 1.00 49.18 A N ATOM 1131 CD PRO A 180 25.960 65.088 24.550 1.00 44.48 A C ATOM 1132 CA PRO A 180 26.210 63.158 23.085 1.00 48.80 A C ATOM 1133 CB PRO A 180 25.728 62.726 24.477 1.00 45.89 A C ATOM 1134 CG PRO A 180 26.098 63.873 25.405 1.00 46.52 A C ATOM 1135 C PRO A 180 25.146 62.875 22.044 1.00 46.04 A C ATOM 1136 O PRO A 180 24.287 63.721 21.816 1.00 48.93 A O ATOM 1137 N PHE A 181 25.220 61.714 21.404 1.00 47.43 A N ATOM 1138 CA PHE A 181 24.157 61.268 20.513 1.00 44.84 A C ATOM 1139 CB PHE A 181 24.682 60.254 19.494 1.00 44.55 A C ATOM 1140 CG PHE A 181 25.570 60.850 18.437 1.00 43.70 A C ATOM 1141 CD1 PHE A 181 25.205 62.010 17.773 1.00 47.73 A C ATOM 1142 CD2 PHE A 181 26.764 60.231 18.084 1.00 46.36 A C ATOM 1143 CE1 PHE A 181 26.031 62.551 16.782 1.00 48.34 A C ATOM 1144 CE2 PHE A 181 27.589 60.768 17.097 1.00 43.09 A C ATOM 1145 CZ PHE A 181 27.222 61.926 16.448 1.00 39.86 A C ATOM 1146 C PHE A 181 23.079 60.645 21.383 1.00 40.91 A C ATOM 1147 O PHE A 181 23.260 60.537 22.593 1.00 39.38 A O ATOM 1148 N ASP A 182 21.979 60.205 20.775 1.00 40.48 A N ATOM 1149 CA ASP A 182 20.780 59.868 21.544 1.00 32.94 A C ATOM 1150 CB ASP A 182 19.733 60.963 21.337 1.00 30.65 A C ATOM 1151 CG ASP A 182 19.144 60.948 19.934 1.00 38.96 A C ATOM 1152 OD1 ASP A 182 19.320 59.953 19.218 1.00 43.10 A O ATOM 1153 OD2 ASP A 182 18.491 61.923 19.538 1.00 45.36 A O ATOM 1154 C ASP A 182 20.148 58.490 21.258 1.00 41.29 A C ATOM 1155 O ASP A 182 18.933 58.318 21.393 1.00 40.40 A O ATOM 1156 N GLY A 183 20.954 57.505 20.874 1.00 38.80 A N ATOM 1157 CA GLY A 183 20.415 56.187 20.582 1.00 42.57 A C ATOM 1158 C GLY A 183 19.895 56.138 19.159 1.00 45.31 A C ATOM 1159 O GLY A 183 20.280 56.953 18.339 1.00 42.68 A O ATOM 1160 N LYS A 184 19.020 55.193 18.852 1.00 44.75 A N ATOM 1161 CA LYS A 184 18.493 55.111 17.496 1.00 46.56 A C ATOM 1162 CB LYS A 184 17.885 53.737 17.229 1.00 47.90 A C ATOM 1163 CG LYS A 184 17.828 53.399 15.757 1.00 51.43 A C ATOM 1164 CD LYS A 184 17.063 52.123 15.508 1.00 43.50 A C ATOM 1165 CE LYS A 184 15.609 52.311 15.832 1.00 44.30 A C ATOM 1166 NZ LYS A 184 14.780 51.494 14.917 1.00 44.04 A N ATOM 1167 C LYS A 184 17.460 56.206 17.230 1.00 49.04 A C ATOM 1168 O LYS A 184 16.738 56.623 18.139 1.00 49.51 A O ATOM 1169 N ASP A 185 17.399 56.656 15.976 1.00 49.36 A N ATOM 1170 CA ASP A 185 16.516 57.746 15.543 1.00 46.30 A C ATOM 1171 CB ASP A 185 15.049 57.327 15.646 1.00 45.98 A C ATOM 1172 CG ASP A 185 14.745 56.085 14.838 1.00 47.99 A C ATOM 1173 OD1 ASP A 185 15.291 55.959 13.718 1.00 42.26 A O ATOM 1174 OD2 ASP A 185 13.967 55.234 15.325 1.00 47.18 A O ATOM 1175 C ASP A 185 16.761 59.067 16.286 1.00 48.11 A C ATOM 1176 O ASP A 185 17.532 59.125 17.236 1.00 50.32 A O ATOM 1177 N GLY A 186 16.093 60.130 15.856 1.00 54.19 A N ATOM 1178 CA GLY A 186 16.308 61.436 16.457 1.00 50.40 A C ATOM 1179 C GLY A 186 17.568 62.043 15.881 1.00 48.45 A C ATOM 1180 O GLY A 186 17.758 62.041 14.667 1.00 50.84 A O ATOM 1181 N LEU A 187 18.430 62.559 16.749 1.00 42.98 A N ATOM 1182 CA LEU A 187 19.743 63.044 16.336 1.00 42.88 A C ATOM 1183 CB LEU A 187 20.606 63.276 17.571 1.00 41.34 A C ATOM 1184 CG LEU A 187 20.675 64.673 18.166 1.00 43.23 A C ATOM 1185 CD1 LEU A 187 19.445 65.449 17.810 1.00 42.58 A C ATOM 1186 CD2 LEU A 187 20.847 64.565 19.681 1.00 44.87 A C ATOM 1187 C LEU A 187 20.488 62.062 15.430 1.00 45.38 A C ATOM 1188 O LEU A 187 21.133 61.148 15.931 1.00 52.68 A O ATOM 1189 N LEU A 188 20.447 62.267 14.114 1.00 38.62 A N ATOM 1190 CA LEU A 188 21.155 61.385 13.185 1.00 39.56 A C ATOM 1191 CB LEU A 188 20.529 61.459 11.794 1.00 38.44 A C ATOM 1192 CG LEU A 188 19.057 61.055 11.716 1.00 40.21 A C ATOM 1193 CD1 LEU A 188 18.620 60.886 10.258 1.00 32.66 A C ATOM 1194 CD2 LEU A 188 18.826 59.778 12.521 1.00 40.60 A C ATOM 1195 C LEU A 188 22.661 61.657 13.077 1.00 43.46 A C ATOM 1196 O LEU A 188 23.427 60.771 12.683 1.00 40.76 A O ATOM 1197 N ALA A 189 23.075 62.873 13.433 1.00 41.09 A N ATOM 1198 CA ALA A 189 24.455 63.319 13.241 1.00 36.56 A C ATOM 1199 CB ALA A 189 24.957 62.871 11.885 1.00 35.84 A C ATOM 1200 C ALA A 189 24.586 64.848 13.366 1.00 40.35 A C ATOM 1201 O ALA A 189 23.588 65.574 13.359 1.00 38.41 A O ATOM 1202 N HIS A 190 25.818 65.336 13.474 1.00 37.22 A N ATOM 1203 CA HIS A 190 26.054 66.772 13.517 1.00 38.14 A C ATOM 1204 CB HIS A 190 25.901 67.332 14.934 1.00 33.23 A C ATOM 1205 CG HIS A 190 26.741 66.638 15.954 1.00 38.68 A C ATOM 1206 CD2 HIS A 190 27.971 66.082 15.868 1.00 41.77 A C ATOM 1207 ND1 HIS A 190 26.325 66.451 17.255 1.00 46.93 A N ATOM 1208 CE1 HIS A 190 27.267 65.816 17.929 1.00 43.47 A C ATOM 1209 NE2 HIS A 190 28.275 65.578 17.109 1.00 44.52 A N ATOM 1210 C HIS A 190 27.418 67.147 12.959 1.00 39.39 A C ATOM 1211 O HIS A 190 28.196 66.285 12.572 1.00 39.30 A O ATOM 1212 N ALA A 191 27.696 68.445 12.926 1.00 40.82 A N ATOM 1213 CA ALA A 191 28.949 68.946 12.386 1.00 42.76 A C ATOM 1214 CB ALA A 191 28.918 68.931 10.858 1.00 33.63 A C ATOM 1215 C ALA A 191 29.203 70.354 12.894 1.00 43.32 A C ATOM 1216 O ALA A 191 28.283 71.040 13.336 1.00 39.36 A O ATOM 1217 N PHE A 192 30.455 70.783 12.808 1.00 40.08 A N ATOM 1218 CA PHE A 192 30.836 72.113 13.264 1.00 47.02 A C ATOM 1219 CB PHE A 192 31.853 72.003 14.398 1.00 52.19 A C ATOM 1220 CG PHE A 192 31.477 70.994 15.459 1.00 50.96 A C ATOM 1221 CD1 PHE A 192 31.128 71.401 16.752 1.00 42.41 A C ATOM 1222 CD2 PHE A 192 31.410 69.641 15.159 1.00 45.70 A C ATOM 1223 CE1 PHE A 192 30.872 70.483 17.721 1.00 46.17 A C ATOM 1224 CE2 PHE A 192 31.076 68.721 16.123 1.00 46.33 A C ATOM 1225 CZ PHE A 192 30.808 69.141 17.409 1.00 51.20 A C ATOM 1226 C PHE A 192 31.390 72.957 12.110 1.00 45.78 A C ATOM 1227 O PHE A 192 31.872 72.416 11.114 1.00 40.80 A O ATOM 1228 N PRO A 193 31.317 74.289 12.243 1.00 43.17 A N ATOM 1229 CD PRO A 193 30.983 75.020 13.472 1.00 38.91 A C ATOM 1230 CA PRO A 193 31.669 75.196 11.147 1.00 43.15 A C ATOM 1231 CB PRO A 193 31.036 76.530 11.570 1.00 39.55 A C ATOM 1232 CG PRO A 193 30.417 76.290 12.941 1.00 44.50 A C ATOM 1233 C PRO A 193 33.173 75.379 11.011 1.00 46.27 A C ATOM 1234 O PRO A 193 33.916 75.105 11.955 1.00 44.43 A O ATOM 1235 N PRO A 194 33.618 75.849 9.837 1.00 47.37 A N ATOM 1236 CD PRO A 194 32.765 76.132 8.668 1.00 44.45 A C ATOM 1237 CA PRO A 194 35.019 76.172 9.572 1.00 46.13 A C ATOM 1238 CB PRO A 194 34.917 77.145 8.401 1.00 47.86 A C ATOM 1239 CG PRO A 194 33.743 76.649 7.640 1.00 43.53 A C ATOM 1240 C PRO A 194 35.691 76.845 10.764 1.00 44.39 A C ATOM 1241 O PRO A 194 35.095 77.705 11.407 1.00 46.02 A O ATOM 1242 N GLY A 195 36.927 76.438 11.038 1.00 48.80 A N ATOM 1243 CA GLY A 195 37.696 76.932 12.164 1.00 44.23 A C ATOM 1244 C GLY A 195 38.759 75.929 12.589 1.00 41.82 A C ATOM 1245 O GLY A 195 38.971 74.914 11.924 1.00 44.40 A O ATOM 1246 N PRO A 196 39.426 76.196 13.716 1.00 39.23 A N ATOM 1247 CD PRO A 196 39.130 77.260 14.684 1.00 41.48 A C ATOM 1248 CA PRO A 196 40.522 75.343 14.172 1.00 37.87 A C ATOM 1249 CB PRO A 196 41.296 76.261 15.124 1.00 44.70 A C ATOM 1250 CG PRO A 196 40.459 77.532 15.272 1.00 45.30 A C ATOM 1251 C PRO A 196 40.049 74.124 14.961 1.00 45.46 A C ATOM 1252 O PRO A 196 39.067 74.191 15.701 1.00 50.75 A O ATOM 1253 N GLY A 197 40.754 73.015 14.805 1.00 41.97 A N ATOM 1254 CA GLY A 197 40.621 71.909 15.729 1.00 46.98 A C ATOM 1255 C GLY A 197 39.394 71.058 15.530 1.00 51.92 A C ATOM 1256 O GLY A 197 39.311 70.297 14.574 1.00 59.06 A O ATOM 1257 N ILE A 198 38.445 71.172 16.447 1.00 53.68 A N ATOM 1258 CA ILE A 198 37.214 70.397 16.358 1.00 51.83 A C ATOM 1259 CB ILE A 198 36.466 70.367 17.705 1.00 45.75 A C ATOM 1260 CG2 ILE A 198 35.817 71.730 17.994 1.00 43.76 A C ATOM 1261 CG1 ILE A 198 35.433 69.243 17.709 1.00 48.71 A C ATOM 1262 CD1 ILE A 198 34.522 69.261 18.916 1.00 45.63 A C ATOM 1263 C ILE A 198 36.292 70.965 15.276 1.00 54.74 A C ATOM 1264 O ILE A 198 35.532 70.228 14.645 1.00 51.87 A O ATOM 1265 N GLN A 199 36.358 72.278 15.067 1.00 46.95 A N ATOM 1266 CA GLN A 199 35.524 72.909 14.061 1.00 48.44 A C ATOM 1267 CB GLN A 199 35.799 74.411 14.008 1.00 47.85 A C ATOM 1268 CG GLN A 199 35.732 75.074 15.373 1.00 46.69 A C ATOM 1269 CD GLN A 199 35.703 76.593 15.312 1.00 45.00 A C ATOM 1270 OE1 GLN A 199 35.431 77.181 14.269 1.00 40.14 A O ATOM 1271 NE2 GLN A 199 35.978 77.232 16.443 1.00 44.81 A N ATOM 1272 C GLN A 199 35.802 72.239 12.722 1.00 47.45 A C ATOM 1273 O GLN A 199 36.880 71.705 12.517 1.00 50.18 A O ATOM 1274 N GLY A 200 34.822 72.236 11.826 1.00 44.72 A N ATOM 1275 CA GLY A 200 34.968 71.560 10.552 1.00 39.34 A C ATOM 1276 C GLY A 200 34.668 70.070 10.619 1.00 43.86 A C ATOM 1277 O GLY A 200 34.507 69.426 9.577 1.00 40.38 A O ATOM 1278 N ASP A 201 34.601 69.526 11.837 1.00 36.55 A N ATOM 1279 CA ASP A 201 34.309 68.105 12.061 1.00 40.58 A C ATOM 1280 CB ASP A 201 34.674 67.692 13.489 1.00 45.61 A C ATOM 1281 CG ASP A 201 36.158 67.587 13.705 1.00 49.67 A C ATOM 1282 OD1 ASP A 201 36.911 67.743 12.722 1.00 52.73 A O ATOM 1283 OD2 ASP A 201 36.569 67.346 14.865 1.00 53.94 A O ATOM 1284 C ASP A 201 32.852 67.684 11.810 1.00 37.16 A C ATOM 1285 O ASP A 201 31.915 68.452 11.995 1.00 34.15 A O ATOM 1286 N ALA A 202 32.688 66.429 11.420 1.00 38.87 A N ATOM 1287 CA ALA A 202 31.381 65.855 11.159 1.00 42.26 A C ATOM 1288 CB ALA A 202 31.188 65.672 9.650 1.00 38.60 A C ATOM 1289 C ALA A 202 31.266 64.516 11.884 1.00 36.65 A C ATOM 1290 O ALA A 202 32.114 63.644 11.722 1.00 41.29 A O ATOM 1291 N HIS A 203 30.232 64.348 12.692 1.00 35.83 A N ATOM 1292 CA HIS A 203 30.055 63.082 13.405 1.00 41.65 A C ATOM 1293 CB HIS A 203 30.212 63.288 14.913 1.00 41.30 A C ATOM 1294 CG HIS A 203 31.529 63.882 15.303 1.00 42.82 A C ATOM 1295 CD2 HIS A 203 32.759 63.760 14.751 1.00 47.56 A C ATOM 1296 ND1 HIS A 203 31.676 64.734 16.376 1.00 46.26 A N ATOM 1297 CE1 HIS A 203 32.939 65.106 16.474 1.00 49.13 A C ATOM 1298 NE2 HIS A 203 33.618 64.532 15.497 1.00 53.43 A N ATOM 1299 C HIS A 203 28.719 62.418 13.095 1.00 38.12 A C ATOM 1300 O HIS A 203 27.703 63.097 12.963 1.00 36.17 A O ATOM 1301 N PHE A 204 28.726 61.092 12.985 1.00 35.39 A N ATOM 1302 CA PHE A 204 27.510 60.331 12.684 1.00 39.06 A C ATOM 1303 CB PHE A 204 27.654 59.584 11.357 1.00 39.49 A C ATOM 1304 CG PHE A 204 28.072 60.465 10.216 1.00 39.87 A C ATOM 1305 CD1 PHE A 204 29.403 60.616 9.894 1.00 41.52 A C ATOM 1306 CD2 PHE A 204 27.134 61.156 9.479 1.00 38.67 A C ATOM 1307 CE1 PHE A 204 29.790 61.438 8.850 1.00 41.34 A C ATOM 1308 CE2 PHE A 204 27.518 61.976 8.433 1.00 38.86 A C ATOM 1309 CZ PHE A 204 28.844 62.114 8.120 1.00 38.16 A C ATOM 1310 C PHE A 204 27.138 59.351 13.798 1.00 43.64 A C ATOM 1311 O PHE A 204 28.002 58.645 14.329 1.00 41.07 A O ATOM 1312 N ASP A 205 25.848 59.315 14.140 1.00 43.29 A N ATOM 1313 CA ASP A 205 25.339 58.443 15.198 1.00 42.38 A C ATOM 1314 CB ASP A 205 23.923 58.858 15.622 1.00 47.87 A C ATOM 1315 CG ASP A 205 23.453 58.154 16.901 1.00 44.18 A C ATOM 1316 OD1 ASP A 205 24.003 57.092 17.264 1.00 41.91 A O ATOM 1317 OD2 ASP A 205 22.532 58.674 17.554 1.00 37.51 A O ATOM 1318 C ASP A 205 25.331 56.978 14.776 1.00 46.02 A C ATOM 1319 O ASP A 205 24.429 56.535 14.060 1.00 40.67 A O ATOM 1320 N ASP A 206 26.326 56.230 15.257 1.00 47.23 A N ATOM 1321 CA ASP A 206 26.441 54.804 14.973 1.00 44.05 A C ATOM 1322 CB ASP A 206 27.816 54.288 15.396 1.00 43.66 A C ATOM 1323 CG ASP A 206 28.418 53.324 14.380 1.00 43.20 A C ATOM 1324 OD1 ASP A 206 27.718 52.933 13.412 1.00 31.90 A O ATOM 1325 OD2 ASP A 206 29.605 52.966 14.553 1.00 46.28 A O ATOM 1326 C ASP A 206 25.335 53.942 15.604 1.00 42.55 A C ATOM 1327 O ASP A 206 25.268 52.742 15.356 1.00 45.05 A O ATOM 1328 N ASP A 207 24.468 54.536 16.415 1.00 39.56 A N ATOM 1329 CA ASP A 207 23.284 53.807 16.845 1.00 39.78 A C ATOM 1330 CB ASP A 207 22.637 54.431 18.089 1.00 42.04 A C ATOM 1331 CG ASP A 207 23.291 53.965 19.400 1.00 44.62 A C ATOM 1332 OD1 ASP A 207 23.795 52.822 19.459 1.00 40.99 A O ATOM 1333 OD2 ASP A 207 23.291 54.742 20.382 1.00 41.45 A O ATOM 1334 C ASP A 207 22.300 53.735 15.680 1.00 43.55 A C ATOM 1335 O ASP A 207 21.325 52.997 15.734 1.00 50.68 A O ATOM 1336 N GLU A 208 22.563 54.489 14.616 1.00 39.96 A N ATOM 1337 CA GLU A 208 21.743 54.390 13.407 1.00 40.53 A C ATOM 1338 CB GLU A 208 21.750 55.700 12.622 1.00 43.15 A C ATOM 1339 CG GLU A 208 21.248 56.888 13.398 1.00 46.47 A C ATOM 1340 CD GLU A 208 19.883 56.640 13.985 1.00 48.59 A C ATOM 1341 OE1 GLU A 208 19.107 55.870 13.378 1.00 49.85 A O ATOM 1342 OE2 GLU A 208 19.590 57.213 15.050 1.00 43.79 A O ATOM 1343 C GLU A 208 22.225 53.280 12.493 1.00 39.47 A C ATOM 1344 O GLU A 208 23.420 52.991 12.428 1.00 40.89 A O ATOM 1345 N LEU A 209 21.289 52.656 11.788 1.00 38.73 A N ATOM 1346 CA LEU A 209 21.639 51.702 10.749 1.00 33.34 A C ATOM 1347 CB LEU A 209 20.471 50.771 10.448 1.00 34.57 A C ATOM 1348 CG LEU A 209 20.713 49.720 9.360 1.00 38.77 A C ATOM 1349 CD1 LEU A 209 21.624 48.607 9.880 1.00 37.95 A C ATOM 1350 CD2 LEU A 209 19.393 49.156 8.832 1.00 38.30 A C ATOM 1351 C LEU A 209 21.994 52.495 9.501 1.00 42.87 A C ATOM 1352 O LEU A 209 21.135 53.146 8.899 1.00 41.83 A O ATOM 1353 N TRP A 210 23.261 52.447 9.112 1.00 38.25 A N ATOM 1354 CA TRP A 210 23.705 53.226 7.973 1.00 43.88 A C ATOM 1355 CB TRP A 210 25.107 53.788 8.224 1.00 41.32 A C ATOM 1356 CG TRP A 210 25.041 54.876 9.226 1.00 37.97 A C ATOM 1357 CD2 TRP A 210 24.492 56.182 9.023 1.00 43.27 A C ATOM 1358 CE2 TRP A 210 24.596 56.872 10.245 1.00 41.98 A C ATOM 1359 CE3 TRP A 210 23.931 56.841 7.916 1.00 39.09 A C ATOM 1360 CD1 TRP A 210 25.421 54.817 10.528 1.00 37.80 A C ATOM 1361 NE1 TRP A 210 25.170 56.016 11.149 1.00 39.60 A N ATOM 1362 CZ2 TRP A 210 24.162 58.194 10.395 1.00 41.39 A C ATOM 1363 CZ3 TRP A 210 23.507 58.150 8.067 1.00 32.20 A C ATOM 1364 CH2 TRP A 210 23.621 58.812 9.294 1.00 32.06 A C ATOM 1365 C TRP A 210 23.608 52.440 6.676 1.00 41.51 A C ATOM 1366 O TRP A 210 24.072 51.310 6.593 1.00 45.91 A O ATOM 1367 N SER A 211 22.970 53.039 5.679 1.00 33.23 A N ATOM 1368 CA SER A 211 22.859 52.413 4.373 1.00 40.21 A C ATOM 1369 CB SER A 211 21.563 51.611 4.262 1.00 39.68 A C ATOM 1370 OG SER A 211 20.471 52.457 3.942 1.00 46.06 A O ATOM 1371 C SER A 211 22.926 53.451 3.255 1.00 41.77 A C ATOM 1372 O SER A 211 23.502 54.530 3.421 1.00 34.06 A O ATOM 1373 N LEU A 212 22.327 53.112 2.116 1.00 42.77 A N ATOM 1374 CA LEU A 212 22.343 53.979 0.946 1.00 43.28 A C ATOM 1375 CB LEU A 212 23.289 53.407 −0.114 1.00 35.29 A C ATOM 1376 CG LEU A 212 24.523 54.233 −0.457 1.00 41.29 A C ATOM 1377 CD1 LEU A 212 25.467 54.349 0.731 1.00 40.19 A C ATOM 1378 CD2 LEU A 212 25.231 53.616 −1.647 1.00 46.67 A C ATOM 1379 C LEU A 212 20.962 54.171 0.325 1.00 46.44 A C ATOM 1380 O LEU A 212 20.837 54.163 −0.902 1.00 44.76 A O ATOM 1381 N GLY A 213 19.920 54.339 1.140 1.00 48.27 A N ATOM 1382 CA GLY A 213 18.593 54.474 0.560 1.00 51.11 A C ATOM 1383 C GLY A 213 17.354 54.371 1.428 1.00 52.93 A C ATOM 1384 O GLY A 213 17.194 55.173 2.347 1.00 61.33 A O ATOM 1385 N LYS A 389 16.439 53.437 1.155 1.00 58.93 A N ATOM 1386 CA LYS A 389 16.470 52.396 0.104 1.00 58.71 A C ATOM 1387 CB LYS A 389 17.362 52.711 −1.093 1.00 52.00 A C ATOM 1388 CG LYS A 389 16.677 53.601 −2.103 1.00 60.52 A C ATOM 1389 CD LYS A 389 15.224 53.196 −2.304 1.00 56.32 A C ATOM 1390 CE LYS A 389 15.117 51.936 −3.140 1.00 61.88 A C ATOM 1391 NZ LYS A 389 13.757 51.780 −3.721 1.00 64.90 A N ATOM 1392 C LYS A 389 16.751 51.010 0.664 1.00 56.01 A C ATOM 1393 O LYS A 389 17.906 50.625 0.866 1.00 52.42 A O ATOM 1394 N GLY A 390 15.668 50.274 0.902 1.00 48.41 A N ATOM 1395 CA GLY A 390 15.726 49.005 1.594 1.00 48.24 A C ATOM 1396 C GLY A 390 15.502 49.218 3.077 1.00 49.81 A C ATOM 1397 O GLY A 390 14.417 48.961 3.589 1.00 55.54 A O ATOM 1398 N GLN A 391 16.533 49.711 3.757 1.00 46.03 A N ATOM 1399 CA GLN A 391 16.502 49.937 5.197 1.00 48.33 A C ATOM 1400 CB GLN A 391 16.599 48.607 5.951 1.00 45.33 A C ATOM 1401 CG GLN A 391 15.323 47.776 5.913 1.00 49.10 A C ATOM 1402 CD GLN A 391 15.502 46.379 6.468 1.00 44.75 A C ATOM 1403 OE1 GLN A 391 16.220 46.165 7.443 1.00 46.20 A O ATOM 1404 NE2 GLN A 391 14.845 45.415 5.844 1.00 45.38 A N ATOM 1405 C GLN A 391 17.666 50.842 5.596 1.00 50.46 A C ATOM 1406 O GLN A 391 18.653 50.940 4.874 1.00 50.22 A O ATOM 1407 N GLY A 392 17.555 51.498 6.746 1.00 50.15 A N ATOM 1408 CA GLY A 392 18.629 52.347 7.231 1.00 45.79 A C ATOM 1409 C GLY A 392 18.619 53.734 6.623 1.00 47.75 A C ATOM 1410 O GLY A 392 17.886 53.998 5.668 1.00 50.03 A O ATOM 1411 N TYR A 393 19.437 54.622 7.182 1.00 49.59 A N ATOM 1412 CA TYR A 393 19.568 55.989 6.675 1.00 45.46 A C ATOM 1413 CB TYR A 393 19.813 56.964 7.820 1.00 40.78 A C ATOM 1414 CG TYR A 393 18.657 57.133 8.777 1.00 44.25 A C ATOM 1415 CD1 TYR A 393 17.579 57.955 8.462 1.00 39.29 A C ATOM 1416 CE1 TYR A 393 16.535 58.120 9.339 1.00 36.38 A C ATOM 1417 CD2 TYR A 393 18.657 56.491 10.011 1.00 47.87 A C ATOM 1418 CE2 TYR A 393 17.619 56.653 10.894 1.00 43.12 A C ATOM 1419 CZ TYR A 393 16.563 57.470 10.554 1.00 43.29 A C ATOM 1420 OH TYR A 393 15.527 57.625 11.439 1.00 50.95 A O ATOM 1421 C TYR A 393 20.721 56.117 5.689 1.00 40.40 A C ATOM 1422 O TYR A 393 21.827 55.646 5.959 1.00 44.20 A O ATOM 1423 N SER A 394 20.460 56.776 4.564 1.00 34.38 A N ATOM 1424 CA SER A 394 21.477 57.012 3.546 1.00 36.71 A C ATOM 1425 CB SER A 394 20.864 57.725 2.337 1.00 40.29 A C ATOM 1426 OG SER A 394 21.831 57.964 1.326 1.00 35.94 A O ATOM 1427 C SER A 394 22.685 57.800 4.068 1.00 35.66 A C ATOM 1428 O SER A 394 22.607 59.006 4.312 1.00 37.53 A O ATOM 1429 N LEU A 395 23.805 57.107 4.233 1.00 35.78 A N ATOM 1430 CA LEU A 395 25.043 57.747 4.647 1.00 35.26 A C ATOM 1431 CB LEU A 395 26.175 56.722 4.706 1.00 30.65 A C ATOM 1432 CG LEU A 395 27.525 57.239 5.202 1.00 32.19 A C ATOM 1433 CD1 LEU A 395 27.367 57.950 6.534 1.00 32.51 A C ATOM 1434 CD2 LEU A 395 28.504 56.096 5.315 1.00 32.07 A C ATOM 1435 C LEU A 395 25.411 58.861 3.676 1.00 35.39 A C ATOM 1436 O LEU A 395 25.864 59.935 4.078 1.00 34.99 A O ATOM 1437 N PHE A 396 25.224 58.588 2.392 1.00 32.75 A N ATOM 1438 CA PHE A 396 25.540 59.556 1.357 1.00 35.29 A C ATOM 1439 CB PHE A 396 25.197 58.986 −0.030 1.00 36.22 A C ATOM 1440 CG PHE A 396 25.196 60.011 −1.126 1.00 32.91 A C ATOM 1441 CD1 PHE A 396 26.307 60.815 −1.348 1.00 35.89 A C ATOM 1442 CD2 PHE A 396 24.089 60.172 −1.936 1.00 32.31 A C ATOM 1443 CE1 PHE A 396 26.310 61.766 −2.359 1.00 36.84 A C ATOM 1444 CE2 PHE A 396 24.081 61.117 −2.953 1.00 34.84 A C ATOM 1445 CZ PHE A 396 25.194 61.919 −3.163 1.00 33.16 A C ATOM 1446 C PHE A 396 24.810 60.873 1.619 1.00 34.29 A C ATOM 1447 O PHE A 396 25.432 61.934 1.703 1.00 34.28 A O ATOM 1448 N LEU A 397 23.494 60.792 1.783 1.00 35.67 A N ATOM 1449 CA LEU A 397 22.660 61.981 1.950 1.00 35.88 A C ATOM 1450 CB LEU A 397 21.180 61.615 1.870 1.00 34.40 A C ATOM 1451 CG LEU A 397 20.674 61.326 0.452 1.00 34.88 A C ATOM 1452 CD1 LEU A 397 19.210 60.907 0.469 1.00 40.43 A C ATOM 1453 CD2 LEU A 397 20.865 62.540 −0.438 1.00 34.70 A C ATOM 1454 C LEU A 397 22.960 62.777 3.218 1.00 31.17 A C ATOM 1455 O LEU A 397 23.138 63.988 3.157 1.00 31.77 A O ATOM 1456 N VAL A 398 23.021 62.100 4.359 1.00 28.52 A N ATOM 1457 CA VAL A 398 23.309 62.773 5.619 1.00 28.45 A C ATOM 1458 CB VAL A 398 23.225 61.791 6.828 1.00 29.92 A C ATOM 1459 CG1 VAL A 398 23.804 62.410 8.076 1.00 27.08 A C ATOM 1460 CG2 VAL A 398 21.787 61.371 7.084 1.00 28.79 A C ATOM 1461 C VAL A 398 24.676 63.469 5.558 1.00 36.34 A C ATOM 1462 O VAL A 398 24.859 64.556 6.123 1.00 33.44 A O ATOM 1463 N ALA A 399 25.624 62.855 4.849 1.00 34.76 A N ATOM 1464 CA ALA A 399 26.975 63.407 4.736 1.00 33.33 A C ATOM 1465 CB ALA A 399 27.932 62.401 4.105 1.00 29.37 A C ATOM 1466 C ALA A 399 26.984 64.714 3.956 1.00 34.30 A C ATOM 1467 O ALA A 399 27.700 65.648 4.311 1.00 34.81 A O ATOM 1468 N ALA A 400 26.201 64.772 2.885 1.00 34.76 A N ATOM 1469 CA ALA A 400 26.103 65.991 2.098 1.00 31.73 A C ATOM 1470 CB ALA A 400 25.190 65.781 0.910 1.00 26.46 A C ATOM 1471 C ALA A 400 25.593 67.126 2.992 1.00 36.30 A C ATOM 1472 O ALA A 400 26.113 68.252 2.974 1.00 33.48 A O ATOM 1473 N HIS A 401 24.587 66.814 3.796 1.00 31.57 A N ATOM 1474 CA HIS A 401 24.048 67.796 4.720 1.00 35.82 A C ATOM 1475 CB HIS A 401 22.845 67.210 5.459 1.00 33.23 A C ATOM 1476 CG HIS A 401 22.192 68.171 6.395 1.00 36.48 A C ATOM 1477 CD2 HIS A 401 22.381 68.395 7.719 1.00 33.26 A C ATOM 1478 ND1 HIS A 401 21.207 69.047 5.992 1.00 34.67 A N ATOM 1479 CE1 HIS A 401 20.825 69.777 7.026 1.00 37.95 A C ATOM 1480 NE2 HIS A 401 21.517 69.396 8.086 1.00 31.50 A N ATOM 1481 C HIS A 401 25.112 68.285 5.714 1.00 35.06 A C ATOM 1482 O HIS A 401 25.343 69.492 5.846 1.00 33.07 A O ATOM 1483 N GLU A 402 25.764 67.344 6.395 1.00 30.51 A N ATOM 1484 CA GLU A 402 26.746 67.674 7.421 1.00 26.51 A C ATOM 1485 CB GLU A 402 27.220 66.417 8.146 1.00 33.83 A C ATOM 1486 CG GLU A 402 26.123 65.652 8.851 1.00 29.47 A C ATOM 1487 CD GLU A 402 25.396 66.497 9.863 1.00 32.53 A C ATOM 1488 OE1 GLU A 402 25.936 67.550 10.265 1.00 31.93 A O ATOM 1489 OE2 GLU A 402 24.282 66.106 10.262 1.00 36.15 A O ATOM 1490 C GLU A 402 27.943 68.424 6.877 1.00 30.27 A C ATOM 1491 O GLU A 402 28.324 69.440 7.438 1.00 35.27 A O ATOM 1492 N PHE A 403 28.544 67.915 5.797 1.00 35.22 A N ATOM 1493 CA PHE A 403 29.620 68.621 5.089 1.00 33.75 A C ATOM 1494 CB PHE A 403 30.033 67.890 3.805 1.00 33.76 A C ATOM 1495 CG PHE A 403 30.615 66.515 4.037 1.00 40.84 A C ATOM 1496 CD1 PHE A 403 31.083 66.141 5.292 1.00 39.95 A C ATOM 1497 CD2 PHE A 403 30.711 65.604 2.992 1.00 35.68 A C ATOM 1498 CE1 PHE A 403 31.607 64.883 5.502 1.00 38.52 A C ATOM 1499 CE2 PHE A 403 31.239 64.344 3.193 1.00 34.41 A C ATOM 1500 CZ PHE A 403 31.690 63.982 4.446 1.00 40.32 A C ATOM 1501 C PHE A 403 29.212 70.047 4.745 1.00 34.69 A C ATOM 1502 O PHE A 403 30.019 70.976 4.832 1.00 36.13 A O ATOM 1503 N GLY A 404 27.957 70.214 4.341 1.00 32.69 A N ATOM 1504 CA GLY A 404 27.398 71.536 4.146 1.00 35.84 A C ATOM 1505 C GLY A 404 27.670 72.414 5.351 1.00 34.68 A C ATOM 1506 O GLY A 404 28.132 73.543 5.213 1.00 35.36 A O ATOM 1507 N HIS A 405 27.381 71.893 6.538 1.00 36.75 A N ATOM 1508 CA HIS A 405 27.696 72.603 7.769 1.00 35.94 A C ATOM 1509 CB HIS A 405 27.244 71.805 8.984 1.00 36.35 A C ATOM 1510 CG HIS A 405 25.796 71.964 9.299 1.00 30.48 A C ATOM 1511 CD2 HIS A 405 24.846 71.053 9.602 1.00 30.12 A C ATOM 1512 ND1 HIS A 405 25.181 73.194 9.339 1.00 36.08 A N ATOM 1513 CE1 HIS A 405 23.905 73.034 9.646 1.00 35.21 A C ATOM 1514 NE2 HIS A 405 23.677 71.746 9.811 1.00 33.13 A N ATOM 1515 C HIS A 405 29.189 72.823 7.865 1.00 40.98 A C ATOM 1516 O HIS A 405 29.660 73.921 8.208 1.00 41.09 A O ATOM 1517 N ALA A 406 29.925 71.759 7.566 1.00 37.81 A N ATOM 1518 CA ALA A 406 31.376 71.763 7.651 1.00 35.81 A C ATOM 1519 CB ALA A 406 31.918 70.404 7.251 1.00 35.22 A C ATOM 1520 C ALA A 406 32.030 72.878 6.821 1.00 35.82 A C ATOM 1521 O ALA A 406 33.148 73.295 7.115 1.00 41.89 A O ATOM 1522 N LEU A 407 31.340 73.357 5.793 1.00 32.88 A N ATOM 1523 CA LEU A 407 31.863 74.450 4.971 1.00 37.46 A C ATOM 1524 CB LEU A 407 31.448 74.287 3.509 1.00 33.28 A C ATOM 1525 CG LEU A 407 31.871 73.041 2.753 1.00 36.50 A C ATOM 1526 CD1 LEU A 407 31.136 73.008 1.437 1.00 40.30 A C ATOM 1527 CD2 LEU A 407 33.383 73.006 2.544 1.00 38.27 A C ATOM 1528 C LEU A 407 31.381 75.813 5.444 1.00 38.99 A C ATOM 1529 O LEU A 407 31.879 76.839 4.992 1.00 43.22 A O ATOM 1530 N GLY A 408 30.380 75.824 6.316 1.00 40.95 A N ATOM 1531 CA GLY A 408 29.880 77.069 6.862 1.00 39.97 A C ATOM 1532 C GLY A 408 28.403 77.337 6.620 1.00 39.95 A C ATOM 1533 O GLY A 408 27.949 78.459 6.841 1.00 42.55 A O ATOM 1534 N LEU A 409 27.649 76.330 6.178 1.00 36.74 A N ATOM 1535 CA LEU A 409 26.213 76.522 5.920 1.00 34.59 A C ATOM 1536 CB LEU A 409 25.705 75.606 4.803 1.00 35.58 A C ATOM 1537 CG LEU A 409 26.195 75.953 3.391 1.00 39.33 A C ATOM 1538 CD1 LEU A 409 25.795 74.878 2.384 1.00 30.99 A C ATOM 1539 CD2 LEU A 409 25.714 77.345 2.953 1.00 30.29 A C ATOM 1540 C LEU A 409 25.341 76.352 7.150 1.00 34.47 A C ATOM 1541 O LEU A 409 25.643 75.564 8.041 1.00 38.48 A O ATOM 1542 N ASP A 410 24.251 77.109 7.184 1.00 39.57 A N ATOM 1543 CA ASP A 410 23.232 76.980 8.220 1.00 35.25 A C ATOM 1544 CB ASP A 410 22.804 78.354 8.704 1.00 30.26 A C ATOM 1545 CG ASP A 410 23.705 78.887 9.762 1.00 35.55 A C ATOM 1546 OD1 ASP A 410 24.120 78.089 10.635 1.00 35.70 A O ATOM 1547 OD2 ASP A 410 23.993 80.098 9.724 1.00 38.32 A O ATOM 1548 C ASP A 410 22.019 76.277 7.656 1.00 35.49 A C ATOM 1549 O ASP A 410 21.814 76.260 6.443 1.00 39.27 A O ATOM 1550 N HIS A 411 21.196 75.716 8.531 1.00 40.76 A N ATOM 1551 CA HIS A 411 20.007 75.014 8.071 1.00 34.38 A C ATOM 1552 CB HIS A 411 19.138 74.561 9.240 1.00 34.73 A C ATOM 1553 CG HIS A 411 19.667 73.356 9.949 1.00 37.49 A C ATOM 1554 CD2 HIS A 411 20.366 72.289 9.493 1.00 33.75 A C ATOM 1555 ND1 HIS A 411 19.511 73.162 11.307 1.00 38.96 A N ATOM 1556 CE1 HIS A 411 20.083 72.024 11.656 1.00 35.88 A C ATOM 1557 NE2 HIS A 411 20.607 71.474 10.574 1.00 40.17 A N ATOM 1558 C HIS A 411 19.201 75.897 7.153 1.00 31.87 A C ATOM 1559 O HIS A 411 19.191 77.116 7.297 1.00 30.11 A O ATOM 1560 N SER A 412 18.540 75.266 6.196 1.00 35.46 A N ATOM 1561 CA SER A 412 17.551 75.935 5.371 1.00 36.69 A C ATOM 1562 CB SER A 412 17.599 75.383 3.953 1.00 34.02 A C ATOM 1563 OG SER A 412 16.485 75.838 3.220 1.00 41.39 A O ATOM 1564 C SER A 412 16.154 75.735 5.958 1.00 38.27 A C ATOM 1565 O SER A 412 15.934 74.848 6.780 1.00 38.18 A O ATOM 1566 N SER A 413 15.208 76.567 5.544 1.00 41.43 A N ATOM 1567 CA SER A 413 13.829 76.406 5.986 1.00 39.44 A C ATOM 1568 CB SER A 413 13.278 77.712 6.557 1.00 36.34 A C ATOM 1569 OG SER A 413 13.008 78.639 5.530 1.00 39.77 A O ATOM 1570 C SER A 413 12.984 75.913 4.818 1.00 44.11 A C ATOM 1571 O SER A 413 11.820 75.531 4.990 1.00 40.30 A O ATOM 1572 N VAL A 414 13.594 75.925 3.631 1.00 42.19 A N ATOM 1573 CA VAL A 414 13.012 75.326 2.438 1.00 36.85 A C ATOM 1574 CB VAL A 414 13.850 75.658 1.181 1.00 38.32 A C ATOM 1575 CG1 VAL A 414 13.476 74.753 0.007 1.00 32.58 A C ATOM 1576 CG2 VAL A 414 13.685 77.114 0.805 1.00 32.39 A C ATOM 1577 C VAL A 414 12.990 73.823 2.643 1.00 37.90 A C ATOM 1578 O VAL A 414 14.043 73.199 2.720 1.00 42.69 A O ATOM 1579 N PRO A 415 11.788 73.237 2.734 1.00 38.26 A N ATOM 1580 CD PRO A 415 10.518 73.943 2.526 1.00 36.50 A C ATOM 1581 CA PRO A 415 11.576 71.817 3.043 1.00 40.79 A C ATOM 1582 CB PRO A 415 10.057 71.659 2.921 1.00 38.57 A C ATOM 1583 CG PRO A 415 9.523 73.019 3.138 1.00 33.99 A C ATOM 1584 C PRO A 415 12.286 70.844 2.095 1.00 36.31 A C ATOM 1585 O PRO A 415 12.826 69.838 2.552 1.00 34.21 A O ATOM 1586 N GLU A 416 12.283 71.133 0.798 1.00 38.92 A N ATOM 1587 CA GLU A 416 12.909 70.234 −0.181 1.00 44.14 A C ATOM 1588 CB GLU A 416 12.311 70.428 −1.581 1.00 37.57 A C ATOM 1589 CG GLU A 416 10.792 70.326 −1.633 1.00 37.51 A C ATOM 1590 CD GLU A 416 10.089 71.522 −1.001 1.00 39.22 A C ATOM 1591 OE1 GLU A 416 10.711 72.601 −0.898 1.00 40.32 A O ATOM 1592 OE2 GLU A 416 8.908 71.384 −0.607 1.00 47.65 A O ATOM 1593 C GLU A 416 14.435 70.375 −0.232 1.00 37.98 A C ATOM 1594 O GLU A 416 15.136 69.429 −0.581 1.00 40.50 A O ATOM 1595 N ALA A 417 14.939 71.548 0.123 1.00 31.10 A N ATOM 1596 CA ALA A 417 16.375 71.785 0.151 1.00 35.99 A C ATOM 1597 CB ALA A 417 16.669 73.189 0.659 1.00 36.83 A C ATOM 1598 C ALA A 417 17.118 70.763 0.999 1.00 35.13 A C ATOM 1599 O ALA A 417 16.601 70.277 2.001 1.00 36.76 A O ATOM 1600 N LEU A 418 18.349 70.473 0.590 1.00 35.37 A N ATOM 1601 CA LEU A 418 19.268 69.594 1.312 1.00 35.31 A C ATOM 1602 CB LEU A 418 20.560 69.442 0.503 1.00 30.84 A C ATOM 1603 CG LEU A 418 21.670 68.685 1.230 1.00 39.17 A C ATOM 1604 CD1 LEU A 418 21.404 67.189 1.167 1.00 31.67 A C ATOM 1605 CD2 LEU A 418 23.048 69.015 0.675 1.00 28.61 A C ATOM 1606 C LEU A 418 19.621 70.045 2.744 1.00 35.70 A C ATOM 1607 O LEU A 418 19.780 69.218 3.640 1.00 35.62 A O ATOM 1608 N MET A 419 19.778 71.349 2.949 1.00 36.62 A N ATOM 1609 CA MET A 419 20.157 71.868 4.257 1.00 33.19 A C ATOM 1610 CB MET A 419 20.875 73.212 4.134 1.00 32.16 A C ATOM 1611 CG MET A 419 22.229 73.126 3.477 1.00 32.84 A C ATOM 1612 SD MET A 419 23.266 71.786 4.102 1.00 35.07 A S ATOM 1613 CE MET A 419 23.403 72.198 5.842 1.00 36.84 A C ATOM 1614 C MET A 419 18.945 72.006 5.157 1.00 35.59 A C ATOM 1615 O MET A 419 19.041 72.518 6.267 1.00 39.45 A O ATOM 1616 N TYR A 420 17.796 71.556 4.676 1.00 38.14 A N ATOM 1617 CA TYR A 420 16.644 71.415 5.543 1.00 35.51 A C ATOM 1618 CB TYR A 420 15.441 70.916 4.761 1.00 34.18 A C ATOM 1619 CG TYR A 420 14.145 71.071 5.523 1.00 42.18 A C ATOM 1620 CD1 TYR A 420 13.590 72.327 5.727 1.00 39.06 A C ATOM 1621 CE1 TYR A 420 12.412 72.479 6.416 1.00 38.71 A C ATOM 1622 CD2 TYR A 420 13.477 69.966 6.039 1.00 39.92 A C ATOM 1623 CE2 TYR A 420 12.293 70.112 6.732 1.00 36.93 A C ATOM 1624 CZ TYR A 420 11.767 71.372 6.919 1.00 36.74 A C ATOM 1625 OH TYR A 420 10.589 71.533 7.612 1.00 38.81 A O ATOM 1626 C TYR A 420 17.004 70.399 6.603 1.00 35.69 A C ATOM 1627 O TYR A 420 17.462 69.311 6.266 1.00 34.24 A O ATOM 1628 N PRO A 421 16.763 70.741 7.883 1.00 39.38 A N ATOM 1629 CD PRO A 421 15.884 71.863 8.249 1.00 36.94 A C ATOM 1630 CA PRO A 421 17.209 69.995 9.068 1.00 35.47 A C ATOM 1631 CB PRO A 421 16.575 70.768 10.234 1.00 34.12 A C ATOM 1632 CG PRO A 421 16.228 72.096 9.684 1.00 35.68 A C ATOM 1633 C PRO A 421 16.718 68.555 9.104 1.00 36.41 A C ATOM 1634 O PRO A 421 17.453 67.681 9.551 1.00 37.42 A O ATOM 1635 N MET A 422 15.493 68.306 8.660 1.00 34.14 A N ATOM 1636 CA MET A 422 14.938 66.958 8.753 1.00 42.16 A C ATOM 1637 CB MET A 422 13.408 66.980 8.679 1.00 41.55 A C ATOM 1638 CG MET A 422 12.720 67.703 9.835 1.00 35.20 A C ATOM 1639 SD MET A 422 10.927 67.599 9.674 1.00 42.41 A S ATOM 1640 CE MET A 422 10.417 69.202 10.291 1.00 31.39 A C ATOM 1641 C MET A 422 15.488 66.022 7.686 1.00 41.20 A C ATOM 1642 O MET A 422 15.939 66.467 6.632 1.00 43.90 A O ATOM 1643 N TYR A 423 15.444 64.722 7.970 1.00 45.04 A N ATOM 1644 CA TYR A 423 15.819 63.704 6.989 1.00 42.31 A C ATOM 1645 CB TYR A 423 16.338 62.446 7.677 1.00 40.32 A C ATOM 1646 CG TYR A 423 16.737 61.371 6.704 1.00 35.85 A C ATOM 1647 CD1 TYR A 423 15.805 60.468 6.216 1.00 39.70 A C ATOM 1648 CE1 TYR A 423 16.164 59.484 5.319 1.00 37.36 A C ATOM 1649 CD2 TYR A 423 18.042 61.262 6.262 1.00 33.86 A C ATOM 1650 CE2 TYR A 423 18.414 60.273 5.366 1.00 36.65 A C ATOM 1651 CZ TYR A 423 17.471 59.390 4.900 1.00 34.05 A C ATOM 1652 OH TYR A 423 17.833 58.410 4.015 1.00 34.60 A O ATOM 1653 C TYR A 423 14.662 63.325 6.067 1.00 40.38 A C ATOM 1654 O TYR A 423 13.587 62.928 6.517 1.00 33.70 A O ATOM 1655 N ARG A 424 14.908 63.461 4.770 1.00 43.26 A N ATOM 1656 CA ARG A 424 13.969 63.074 3.730 1.00 33.79 A C ATOM 1657 CB ARG A 424 13.484 64.311 2.969 1.00 36.54 A C ATOM 1658 CG ARG A 424 14.398 64.745 1.800 1.00 43.63 A C ATOM 1659 CD ARG A 424 14.172 66.204 1.401 1.00 49.92 A C ATOM 1660 NE ARG A 424 14.486 66.468 −0.005 1.00 40.25 A N ATOM 1661 CZ ARG A 424 13.690 66.141 −1.023 1.00 41.63 A C ATOM 1662 NH1 ARG A 424 12.539 65.524 −0.796 1.00 43.84 A N ATOM 1663 NH2 ARG A 424 14.042 66.423 −2.271 1.00 43.80 A N ATOM 1664 C ARG A 424 14.787 62.212 2.800 1.00 38.38 A C ATOM 1665 O ARG A 424 15.917 62.567 2.459 1.00 43.07 A O ATOM 1666 N PHE A 425 14.269 61.066 2.394 1.00 35.52 A N ATOM 1667 CA PHE A 425 15.027 60.312 1.416 1.00 34.46 A C ATOM 1668 CB PHE A 425 15.026 58.812 1.672 1.00 35.53 A C ATOM 1669 CG PHE A 425 15.590 58.034 0.523 1.00 36.58 A C ATOM 1670 CD1 PHE A 425 16.958 57.965 0.328 1.00 33.57 A C ATOM 1671 CD2 PHE A 425 14.757 57.430 −0.395 1.00 37.30 A C ATOM 1672 CE1 PHE A 425 17.485 57.272 −0.731 1.00 39.85 A C ATOM 1673 CE2 PHE A 425 15.283 56.740 −1.471 1.00 48.72 A C ATOM 1674 CZ PHE A 425 16.653 56.661 −1.635 1.00 45.38 A C ATOM 1675 C PHE A 425 14.520 60.586 0.016 1.00 36.12 A C ATOM 1676 O PHE A 425 13.326 60.498 −0.252 1.00 43.15 A O ATOM 1677 N THR A 426 15.443 60.911 −0.875 1.00 34.43 A N ATOM 1678 CA THR A 426 15.116 61.156 −2.267 1.00 38.75 A C ATOM 1679 CB THR A 426 15.326 62.641 −2.635 1.00 39.94 A C ATOM 1680 OG1 THR A 426 15.113 62.830 −4.034 1.00 39.18 A O ATOM 1681 CG2 THR A 426 16.728 63.090 −2.286 1.00 28.57 A C ATOM 1682 C THR A 426 16.017 60.299 −3.135 1.00 39.06 A C ATOM 1683 O THR A 426 17.018 59.768 −2.660 1.00 31.83 A O ATOM 1684 N GLU A 427 15.653 60.151 −4.402 1.00 42.55 A N ATOM 1685 CA GLU A 427 16.572 59.571 −5.371 1.00 42.35 A C ATOM 1686 CB GLU A 427 15.968 58.353 −6.051 1.00 42.41 A C ATOM 1687 CG GLU A 427 15.487 57.330 −5.068 1.00 52.95 A C ATOM 1688 CD GLU A 427 15.779 55.931 −5.517 1.00 55.58 A C ATOM 1689 OE1 GLU A 427 14.967 55.373 −6.288 1.00 54.06 A O ATOM 1690 OE2 GLU A 427 16.821 55.394 −5.083 1.00 55.76 A O ATOM 1691 C GLU A 427 16.982 60.619 −6.393 1.00 44.48 A C ATOM 1692 O GLU A 427 17.865 60.388 −7.214 1.00 50.98 A O ATOM 1693 N GLY A 428 16.343 61.781 −6.327 1.00 39.41 A N ATOM 1694 CA GLY A 428 16.704 62.885 −7.188 1.00 38.09 A C ATOM 1695 C GLY A 428 18.002 63.502 −6.723 1.00 39.67 A C ATOM 1696 O GLY A 428 18.466 63.207 −5.617 1.00 39.35 A O ATOM 1697 N PRO A 429 18.599 64.360 −7.567 1.00 42.88 A N ATOM 1698 CD PRO A 429 18.070 64.730 −8.891 1.00 34.17 A C ATOM 1699 CA PRO A 429 19.814 65.112 −7.233 1.00 33.35 A C ATOM 1700 CB PRO A 429 19.894 66.154 −8.350 1.00 28.70 A C ATOM 1701 CG PRO A 429 19.162 65.572 −9.466 1.00 32.70 A C ATOM 1702 C PRO A 429 19.663 65.817 −5.882 1.00 38.50 A C ATOM 1703 O PRO A 429 18.720 66.579 −5.681 1.00 39.95 A O ATOM 1704 N PRO A 430 20.588 65.566 −4.957 1.00 36.40 A N ATOM 1705 CD PRO A 430 21.687 64.587 −5.041 1.00 22.80 A C ATOM 1706 CA PRO A 430 20.441 66.139 −3.614 1.00 33.48 A C ATOM 1707 CB PRO A 430 21.652 65.575 −2.861 1.00 36.60 A C ATOM 1708 CG PRO A 430 22.007 64.309 −3.612 1.00 30.54 A C ATOM 1709 C PRO A 430 20.402 67.677 −3.525 1.00 30.49 A C ATOM 1710 O PRO A 430 19.786 68.175 −2.599 1.00 44.03 A O ATOM 1711 N LEU A 431 21.019 68.418 −4.435 1.00 33.03 A N ATOM 1712 CA LEU A 431 21.093 69.882 −4.285 1.00 32.86 A C ATOM 1713 CB LEU A 431 22.426 70.420 −4.794 1.00 37.62 A C ATOM 1714 CG LEU A 431 23.661 70.087 −3.963 1.00 43.53 A C ATOM 1715 CD1 LEU A 431 24.907 70.687 −4.602 1.00 32.68 A C ATOM 1716 CD2 LEU A 431 23.471 70.590 −2.546 1.00 34.80 A C ATOM 1717 C LEU A 431 19.966 70.652 −4.964 1.00 35.94 A C ATOM 1718 O LEU A 431 19.527 70.301 −6.051 1.00 37.09 A O ATOM 1719 N HIS A 432 19.514 71.718 −4.312 1.00 36.54 A N ATOM 1720 CA HIS A 432 18.453 72.563 −4.845 1.00 33.66 A C ATOM 1721 CB HIS A 432 17.163 72.399 −4.027 1.00 33.15 A C ATOM 1722 CG HIS A 432 16.640 70.996 −3.994 1.00 33.59 A C ATOM 1723 CD2 HIS A 432 15.543 70.439 −4.556 1.00 30.52 A C ATOM 1724 ND1 HIS A 432 17.274 69.981 −3.306 1.00 35.78 A N ATOM 1725 CE1 HIS A 432 16.596 68.857 −3.459 1.00 33.45 A C ATOM 1726 NE2 HIS A 432 15.540 69.108 −4.209 1.00 36.07 A N ATOM 1727 C HIS A 432 18.924 74.014 −4.818 1.00 34.10 A C ATOM 1728 O HIS A 432 19.929 74.328 −4.183 1.00 34.51 A O ATOM 1729 N LYS A 433 18.196 74.889 −5.509 1.00 34.35 A N ATOM 1730 CA LYS A 433 18.593 76.287 −5.678 1.00 32.83 A C ATOM 1731 CB LYS A 433 17.442 77.107 −6.276 1.00 34.11 A C ATOM 1732 CG LYS A 433 17.169 76.814 −7.751 1.00 41.26 A C ATOM 1733 CD LYS A 433 15.725 77.134 −8.145 1.00 33.94 A C ATOM 1734 CE LYS A 433 15.461 76.868 −9.628 1.00 35.87 A C ATOM 1735 NZ LYS A 433 16.383 77.614 −10.533 1.00 32.69 A N ATOM 1736 C LYS A 433 19.061 76.918 −4.376 1.00 36.35 A C ATOM 1737 O LYS A 433 20.087 77.594 −4.336 1.00 35.06 A O ATOM 1738 N ASP A 434 18.313 76.680 −3.306 1.00 33.37 A N ATOM 1739 CA ASP A 434 18.646 77.261 −2.019 1.00 30.23 A C ATOM 1740 CB ASP A 434 17.562 76.969 −0.979 1.00 33.14 A C ATOM 1741 CG ASP A 434 17.698 77.847 0.248 1.00 34.72 A C ATOM 1742 OD1 ASP A 434 17.418 79.056 0.137 1.00 31.97 A O ATOM 1743 OD2 ASP A 434 18.106 77.337 1.312 1.00 35.18 A O ATOM 1744 C ASP A 434 20.004 76.814 −1.493 1.00 30.02 A C ATOM 1745 O ASP A 434 20.721 77.601 −0.898 1.00 32.63 A O ATOM 1746 N ASP A 435 20.352 75.550 −1.698 1.00 32.63 A N ATOM 1747 CA ASP A 435 21.655 75.053 −1.269 1.00 33.52 A C ATOM 1748 CB ASP A 435 21.712 73.521 −1.338 1.00 30.37 A C ATOM 1749 CG ASP A 435 20.584 72.850 −0.569 1.00 38.23 A C ATOM 1750 OD1 ASP A 435 20.380 73.171 0.628 1.00 37.21 A O ATOM 1751 OD2 ASP A 435 19.907 71.979 −1.164 1.00 41.09 A O ATOM 1752 C ASP A 435 22.800 75.684 −2.090 1.00 35.28 A C ATOM 1753 O ASP A 435 23.788 76.153 −1.523 1.00 32.93 A O ATOM 1754 N VAL A 436 22.656 75.695 −3.417 1.00 32.42 A N ATOM 1755 CA VAL A 436 23.667 76.278 −4.303 1.00 33.19 A C ATOM 1756 CB VAL A 436 23.277 76.114 −5.794 1.00 39.80 A C ATOM 1757 CG1 VAL A 436 24.230 76.895 −6.701 1.00 34.36 A C ATOM 1758 CG2 VAL A 436 23.242 74.657 −6.178 1.00 31.56 A C ATOM 1759 C VAL A 436 23.884 77.765 −4.020 1.00 35.14 A C ATOM 1760 O VAL A 436 25.018 78.228 −3.889 1.00 36.16 A O ATOM 1761 N ASN A 437 22.787 78.509 −3.932 1.00 33.33 A N ATOM 1762 CA ASN A 437 22.857 79.933 −3.660 1.00 36.01 A C ATOM 1763 CB ASN A 437 21.482 80.582 −3.788 1.00 34.26 A C ATOM 1764 CG ASN A 437 21.054 80.734 −5.230 1.00 38.90 A C ATOM 1765 OD1 ASN A 437 21.797 80.381 −6.146 1.00 49.61 A O ATOM 1766 ND2 ASN A 437 19.863 81.259 −5.444 1.00 33.73 A N ATOM 1767 C ASN A 437 23.456 80.212 −2.303 1.00 39.47 A C ATOM 1768 O ASN A 437 24.252 81.136 −2.148 1.00 40.70 A O ATOM 1769 N GLY A 438 23.078 79.404 −1.319 1.00 40.20 A N ATOM 1770 CA GLY A 438 23.609 79.560 0.020 1.00 39.49 A C ATOM 1771 C GLY A 438 25.117 79.471 −0.032 1.00 40.21 A C ATOM 1772 O GLY A 438 25.822 80.411 0.344 1.00 48.20 A O ATOM 1773 N ILE A 439 25.616 78.343 −0.521 1.00 37.01 A N ATOM 1774 CA ILE A 439 27.065 78.146 −0.663 1.00 46.85 A C ATOM 1775 CB ILE A 439 27.423 76.690 −1.089 1.00 38.61 A C ATOM 1776 CG2 ILE A 439 27.312 76.523 −2.584 1.00 37.75 A C ATOM 1777 CG1 ILE A 439 28.824 76.314 −0.608 1.00 40.92 A C ATOM 1778 CD1 ILE A 439 29.037 76.507 0.864 1.00 36.99 A C ATOM 1779 C ILE A 439 27.757 79.186 −1.574 1.00 41.38 A C ATOM 1780 O ILE A 439 28.900 79.552 −1.322 1.00 39.86 A O ATOM 1781 N ARG A 440 27.073 79.676 −2.610 1.00 39.37 A N ATOM 1782 CA ARG A 440 27.633 80.779 −3.408 1.00 41.04 A C ATOM 1783 CB ARG A 440 26.747 81.136 −4.605 1.00 33.93 A C ATOM 1784 CG ARG A 440 26.634 80.047 −5.641 1.00 40.37 A C ATOM 1785 CD ARG A 440 26.017 80.567 −6.926 1.00 42.98 A C ATOM 1786 NE ARG A 440 26.963 81.332 −7.737 1.00 45.89 A N ATOM 1787 CZ ARG A 440 26.641 81.941 −8.874 1.00 44.46 A C ATOM 1788 NH1 ARG A 440 25.398 81.879 −9.323 1.00 36.67 A N ATOM 1789 NH2 ARG A 440 27.557 82.609 −9.564 1.00 46.47 A N ATOM 1790 C ARG A 440 27.832 82.027 −2.558 1.00 43.16 A C ATOM 1791 O ARG A 440 28.902 82.626 −2.563 1.00 45.45 A O ATOM 1792 N HIS A 441 26.789 82.414 −1.831 1.00 47.75 A N ATOM 1793 CA HIS A 441 26.806 83.640 −1.040 1.00 47.84 A C ATOM 1794 CB HIS A 441 25.402 83.969 −0.535 1.00 44.88 A C ATOM 1795 CG HIS A 441 24.419 84.235 −1.631 1.00 42.35 A C ATOM 1796 CD2 HIS A 441 23.066 84.160 −1.648 1.00 43.42 A C ATOM 1797 ND1 HIS A 441 24.804 84.652 −2.881 1.00 43.18 A N ATOM 1798 CE1 HIS A 441 23.726 84.811 −3.640 1.00 48.88 A C ATOM 1799 NE2 HIS A 441 22.665 84.525 −2.914 1.00 50.69 A N ATOM 1800 C HIS A 441 27.740 83.545 0.149 1.00 43.15 A C ATOM 1801 O HIS A 441 27.494 84.162 1.173 1.00 47.16 A O ATOM 1802 N LEU A 442 28.807 82.770 0.005 1.00 43.63 A N ATOM 1803 CA LEU A 442 29.724 82.515 1.098 1.00 42.86 A C ATOM 1804 CB LEU A 442 29.351 81.201 1.790 1.00 44.66 A C ATOM 1805 CG LEU A 442 29.809 80.979 3.235 1.00 47.04 A C ATOM 1806 CD1 LEU A 442 28.896 79.993 3.962 1.00 39.21 A C ATOM 1807 CD2 LEU A 442 31.249 80.512 3.280 1.00 51.09 A C ATOM 1808 C LEU A 442 31.133 82.438 0.542 1.00 49.04 A C ATOM 1809 O LEU A 442 32.074 82.938 1.152 1.00 56.86 A O ATOM 1810 N TYR A 443 31.260 81.809 −0.625 1.00 49.44 A N ATOM 1811 CA TYR A 443 32.537 81.655 −1.325 1.00 48.15 A C ATOM 1812 CB TYR A 443 32.930 80.172 −1.425 1.00 43.21 A C ATOM 1813 CG TYR A 443 33.289 79.557 −0.098 1.00 43.91 A C ATOM 1814 CD1 TYR A 443 32.441 78.656 0.523 1.00 46.34 A C ATOM 1815 CE1 TYR A 443 32.763 78.095 1.743 1.00 44.55 A C ATOM 1816 CD2 TYR A 443 34.471 79.890 0.542 1.00 45.27 A C ATOM 1817 CE2 TYR A 443 34.801 79.337 1.763 1.00 47.19 A C ATOM 1818 CZ TYR A 443 33.943 78.443 2.361 1.00 44.06 A C ATOM 1819 OH TYR A 443 34.266 77.895 3.582 1.00 39.32 A O ATOM 1820 C TYR A 443 32.462 82.263 −2.724 1.00 47.20 A C ATOM 1821 O TYR A 443 31.551 81.952 −3.497 1.00 43.08 A O ATOM 1822 ZN ZN A 500 22.173 70.201 9.953 1.00 41.19 A Zn ATOM 1823 ZN ZN A 501 30.204 64.830 18.023 1.00 47.86 A Zn ATOM 1824 CA CA A 502 20.082 59.015 16.980 1.00 50.81 A Ca ATOM 1825 CA CA A 504 39.043 69.999 12.033 1.00 67.22 A Ca ATOM 1826 CB ASP B 41 4.353 14.442 39.527 1.00 77.43 B C ATOM 1827 CG ASP B 41 3.555 14.867 38.310 1.00 77.58 B C ATOM 1828 OD1 ASP B 41 3.156 13.983 37.522 1.00 71.95 B O ATOM 1829 OD2 ASP B 41 3.343 16.086 38.135 1.00 69.04 B O ATOM 1830 C ASP B 41 5.421 16.608 40.239 1.00 68.23 B C ATOM 1831 O ASP B 41 5.803 17.606 39.631 1.00 68.27 B O ATOM 1832 N ASP B 41 6.629 14.446 40.443 1.00 62.78 B N ATOM 1833 CA ASP B 41 5.667 15.211 39.661 1.00 71.10 B C ATOM 1834 N ARG B 42 4.771 16.679 41.399 1.00 68.75 B N ATOM 1835 CA ARG B 42 4.596 17.954 42.097 1.00 68.25 B C ATOM 1836 CB ARG B 42 3.877 17.752 43.430 1.00 63.43 B C ATOM 1837 CG ARG B 42 3.790 19.016 44.288 1.00 67.79 B C ATOM 1838 CD ARG B 42 2.493 19.782 44.032 1.00 73.81 B C ATOM 1839 NE ARG B 42 2.448 21.075 44.718 1.00 72.77 B N ATOM 1840 CZ ARG B 42 1.338 21.792 44.890 1.00 68.09 B C ATOM 1841 NH1 ARG B 42 0.174 21.340 44.434 1.00 60.94 B N ATOM 1842 NH2 ARG B 42 1.390 22.959 45.521 1.00 53.99 B N ATOM 1843 C ARG B 42 5.965 18.560 42.368 1.00 71.79 B C ATOM 1844 O ARG B 42 6.167 19.774 42.263 1.00 61.68 B O ATOM 1845 N GLN B 43 6.900 17.690 42.734 1.00 70.14 B N ATOM 1846 CA GLN B 43 8.270 18.091 42.989 1.00 66.96 B C ATOM 1847 CB GLN B 43 9.109 16.868 43.356 1.00 68.64 B C ATOM 1848 CG GLN B 43 8.321 15.762 44.064 1.00 74.42 B C ATOM 1849 CD GLN B 43 7.705 14.759 43.098 1.00 73.04 B C ATOM 1850 OE1 GLN B 43 8.386 14.220 42.221 1.00 67.06 B O ATOM 1851 NE2 GLN B 43 6.413 14.493 43.269 1.00 65.67 B N ATOM 1852 C GLN B 43 8.808 18.728 41.721 1.00 68.43 B C ATOM 1853 O GLN B 43 9.313 19.856 41.734 1.00 63.99 B O ATOM 1854 N LEU B 44 8.679 17.997 40.620 1.00 62.80 B N ATOM 1855 CA LEU B 44 9.126 18.495 39.339 1.00 58.41 B C ATOM 1856 CB LEU B 44 8.786 17.510 38.220 1.00 59.98 B C ATOM 1857 CG LEU B 44 9.578 17.675 36.918 1.00 64.99 B C ATOM 1858 CD1 LEU B 44 9.738 16.341 36.184 1.00 59.70 B C ATOM 1859 CD2 LEU B 44 8.941 18.726 36.020 1.00 56.49 B C ATOM 1860 C LEU B 44 8.471 19.846 39.107 1.00 61.51 B C ATOM 1861 O LEU B 44 9.121 20.883 39.218 1.00 65.64 B O ATOM 1862 N ALA B 45 7.178 19.831 38.814 1.00 62.18 B N ATOM 1863 CA ALA B 45 6.447 21.060 38.565 1.00 60.13 B C ATOM 1864 CB ALA B 45 4.983 20.878 38.910 1.00 64.37 B C ATOM 1865 C ALA B 45 7.052 22.209 39.363 1.00 61.16 B C ATOM 1866 O ALA B 45 7.513 23.191 38.788 1.00 60.58 B O ATOM 1867 N GLU B 46 7.074 22.065 40.686 1.00 65.00 B N ATOM 1868 CA GLU B 46 7.570 23.112 41.580 1.00 61.96 B C ATOM 1869 CB GLU B 46 7.503 22.655 43.042 1.00 53.91 B C ATOM 1870 CG GLU B 46 6.146 22.859 43.699 1.00 59.21 B C ATOM 1871 CD GLU B 46 6.047 22.212 45.076 1.00 68.20 B C ATOM 1872 OE1 GLU B 46 6.660 21.144 45.290 1.00 66.18 B O ATOM 1873 OE2 GLU B 46 5.348 22.771 45.946 1.00 67.92 B O ATOM 1874 C GLU B 46 8.987 23.563 41.240 1.00 58.57 B C ATOM 1875 O GLU B 46 9.227 24.739 40.958 1.00 57.82 B O ATOM 1876 N GLU B 47 9.925 22.625 41.280 1.00 55.71 B N ATOM 1877 CA GLU B 47 11.328 22.941 41.057 1.00 58.64 B C ATOM 1878 CB GLU B 47 12.159 21.656 41.061 1.00 67.19 B C ATOM 1879 CG GLU B 47 13.631 21.863 41.360 1.00 70.42 B C ATOM 1880 CD GLU B 47 14.331 22.674 40.292 1.00 70.30 B C ATOM 1881 OE1 GLU B 47 14.058 22.436 39.095 1.00 71.02 B O ATOM 1882 OE2 GLU B 47 15.155 23.547 40.649 1.00 73.47 B O ATOM 1883 C GLU B 47 11.512 23.691 39.737 1.00 63.42 B C ATOM 1884 O GLU B 47 12.242 24.682 39.672 1.00 61.20 B O ATOM 1885 N TYR B 48 10.841 23.209 38.693 1.00 57.55 B N ATOM 1886 CA TYR B 48 10.898 23.827 37.374 1.00 60.26 B C ATOM 1887 CB TYR B 48 10.009 23.051 36.397 1.00 57.66 B C ATOM 1888 CG TYR B 48 10.236 23.366 34.934 1.00 57.89 B C ATOM 1889 CD1 TYR B 48 9.789 24.559 34.380 1.00 58.94 B C ATOM 1890 CE1 TYR B 48 9.994 24.848 33.031 1.00 59.51 B C ATOM 1891 CD2 TYR B 48 10.883 22.455 34.098 1.00 61.36 B C ATOM 1892 CE2 TYR B 48 11.090 22.731 32.746 1.00 55.33 B C ATOM 1893 CZ TYR B 48 10.642 23.931 32.220 1.00 57.84 B C ATOM 1894 OH TYR B 48 10.835 24.218 30.884 1.00 53.72 B O ATOM 1895 C TYR B 48 10.470 25.294 37.425 1.00 58.81 B C ATOM 1896 O TYR B 48 11.147 26.170 36.893 1.00 61.87 B O ATOM 1897 N LEU B 49 9.346 25.557 38.075 1.00 56.00 B N ATOM 1898 CA LEU B 49 8.805 26.900 38.135 1.00 54.19 B C ATOM 1899 CB LEU B 49 7.429 26.878 38.788 1.00 61.61 B C ATOM 1900 CG LEU B 49 6.417 25.970 38.096 1.00 62.24 B C ATOM 1901 CD1 LEU B 49 5.155 25.809 38.943 1.00 60.49 B C ATOM 1902 CD2 LEU B 49 6.095 26.522 36.720 1.00 60.19 B C ATOM 1903 C LEU B 49 9.725 27.833 38.906 1.00 57.61 B C ATOM 1904 O LEU B 49 9.804 29.025 38.613 1.00 59.27 B O ATOM 1905 N TYR B 50 10.421 27.307 39.902 1.00 52.94 B N ATOM 1906 CA TYR B 50 11.322 28.164 40.652 1.00 54.50 B C ATOM 1907 CB TYR B 50 11.625 27.603 42.047 1.00 51.82 B C ATOM 1908 CG TYR B 50 12.663 28.438 42.749 1.00 51.29 B C ATOM 1909 CD1 TYR B 50 12.301 29.582 43.439 1.00 55.78 B C ATOM 1910 CE1 TYR B 50 13.250 30.372 44.057 1.00 62.06 B C ATOM 1911 CD2 TYR B 50 14.015 28.120 42.666 1.00 53.44 B C ATOM 1912 CE2 TYR B 50 14.972 28.903 43.276 1.00 55.28 B C ATOM 1913 CZ TYR B 50 14.584 30.028 43.973 1.00 58.76 B C ATOM 1914 OH TYR B 50 15.527 30.817 44.595 1.00 60.81 B O ATOM 1915 C TYR B 50 12.623 28.428 39.884 1.00 56.14 B C ATOM 1916 O TYR B 50 13.121 29.554 39.848 1.00 55.56 B O ATOM 1917 N ARG B 51 13.167 27.383 39.270 1.00 58.15 B N ATOM 1918 CA ARG B 51 14.458 27.477 38.600 1.00 55.92 B C ATOM 1919 CB ARG B 51 14.850 26.126 38.009 1.00 56.07 B C ATOM 1920 CG ARG B 51 16.194 26.148 37.321 1.00 48.94 B C ATOM 1921 CD ARG B 51 16.380 24.960 36.395 1.00 51.62 B C ATOM 1922 NE ARG B 51 16.550 23.693 37.094 1.00 50.21 B N ATOM 1923 CZ ARG B 51 17.631 23.368 37.792 1.00 54.62 B C ATOM 1924 NH1 ARG B 51 18.630 24.230 37.908 1.00 47.29 B N ATOM 1925 NH2 ARG B 51 17.707 22.187 38.388 1.00 63.33 B N ATOM 1926 C ARG B 51 14.470 28.519 37.495 1.00 54.18 B C ATOM 1927 O ARG B 51 15.403 29.315 37.384 1.00 50.10 B O ATOM 1928 N TYR B 52 13.432 28.507 36.672 1.00 53.51 B N ATOM 1929 CA TYR B 52 13.431 29.336 35.477 1.00 49.85 B C ATOM 1930 CB TYR B 52 12.780 28.584 34.310 1.00 44.56 B C ATOM 1931 CG TYR B 52 13.525 27.295 34.025 1.00 43.22 B C ATOM 1932 CD1 TYR B 52 12.927 26.060 34.199 1.00 44.80 B C ATOM 1933 CE1 TYR B 52 13.629 24.894 33.962 1.00 48.47 B C ATOM 1934 CD2 TYR B 52 14.858 27.326 33.631 1.00 42.01 B C ATOM 1935 CE2 TYR B 52 15.562 26.179 33.391 1.00 37.31 B C ATOM 1936 CZ TYR B 52 14.953 24.964 33.555 1.00 48.17 B C ATOM 1937 OH TYR B 52 15.680 23.819 33.312 1.00 49.11 B O ATOM 1938 C TYR B 52 12.817 30.699 35.744 1.00 49.91 B C ATOM 1939 O TYR B 52 12.577 31.476 34.823 1.00 52.36 B O ATOM 1940 N GLY B 53 12.580 30.976 37.024 1.00 53.69 B N ATOM 1941 CA GLY B 53 12.175 32.295 37.484 1.00 58.02 B C ATOM 1942 C GLY B 53 10.683 32.558 37.592 1.00 61.60 B C ATOM 1943 O GLY B 53 10.271 33.694 37.815 1.00 65.26 B O ATOM 1944 N TYR B 54 9.869 31.521 37.443 1.00 55.74 B N ATOM 1945 CA TYR B 54 8.420 31.703 37.411 1.00 60.33 B C ATOM 1946 CB TYR B 54 7.731 30.462 36.841 1.00 60.45 B C ATOM 1947 CG TYR B 54 7.995 30.296 35.369 1.00 60.36 B C ATOM 1948 CD1 TYR B 54 8.746 29.231 34.892 1.00 61.28 B C ATOM 1949 CE1 TYR B 54 9.001 29.088 33.539 1.00 59.44 B C ATOM 1950 CD2 TYR B 54 7.522 31.228 34.457 1.00 58.87 B C ATOM 1951 CE2 TYR B 54 7.773 31.094 33.106 1.00 59.34 B C ATOM 1952 CZ TYR B 54 8.513 30.023 32.653 1.00 55.15 B C ATOM 1953 OH TYR B 54 8.765 29.892 31.309 1.00 58.06 B O ATOM 1954 C TYR B 54 7.809 32.073 38.759 1.00 63.37 B C ATOM 1955 O TYR B 54 7.066 33.047 38.862 1.00 65.68 B O ATOM 1956 N THR B 55 8.113 31.289 39.785 1.00 62.80 B N ATOM 1957 CA THR B 55 7.536 31.513 41.105 1.00 63.55 B C ATOM 1958 CB THR B 55 8.090 30.510 42.143 1.00 61.62 B C ATOM 1959 OG1 THR B 55 9.521 30.565 42.142 1.00 70.91 B O ATOM 1960 CG2 THR B 55 7.657 29.091 41.809 1.00 57.64 B C ATOM 1961 C THR B 55 7.781 32.943 41.595 1.00 69.37 B C ATOM 1962 O THR B 55 6.851 33.646 41.998 1.00 70.84 B O ATOM 1963 N ARG B 56 9.036 33.375 41.545 1.00 66.80 B N ATOM 1964 CA ARG B 56 9.431 34.656 42.120 1.00 64.68 B C ATOM 1965 CB ARG B 56 10.957 34.752 42.177 1.00 74.06 B C ATOM 1966 CG ARG B 56 11.501 36.077 42.685 1.00 84.37 B C ATOM 1967 CD ARG B 56 12.951 35.934 43.122 1.00 85.54 B C ATOM 1968 NE ARG B 56 13.703 37.172 42.943 1.00 87.12 B N ATOM 1969 CZ ARG B 56 15.001 37.296 43.202 1.00 86.97 B C ATOM 1970 NH1 ARG B 56 15.687 36.255 43.659 1.00 81.08 B N ATOM 1971 NH2 ARG B 56 15.612 38.459 43.006 1.00 81.03 B N ATOM 1972 C ARG B 56 8.834 35.860 41.389 1.00 64.25 B C ATOM 1973 O ARG B 56 8.856 36.978 41.898 1.00 66.74 B O ATOM 1974 N VAL B 57 8.298 35.632 40.197 1.00 65.37 B N ATOM 1975 CA VAL B 57 7.650 36.699 39.445 1.00 60.53 B C ATOM 1976 CB VAL B 57 7.718 36.430 37.933 1.00 59.91 B C ATOM 1977 CG1 VAL B 57 6.939 37.474 37.159 1.00 60.10 B C ATOM 1978 CG2 VAL B 57 9.161 36.412 37.480 1.00 62.14 B C ATOM 1979 C VAL B 57 6.197 36.859 39.901 1.00 70.86 B C ATOM 1980 O VAL B 57 5.637 37.961 39.877 1.00 65.59 B O ATOM 1981 N ALA B 58 5.601 35.751 40.334 1.00 70.38 B N ATOM 1982 CA ALA B 58 4.243 35.761 40.863 1.00 66.51 B C ATOM 1983 CB ALA B 58 3.443 34.599 40.290 1.00 66.23 B C ATOM 1984 C ALA B 58 4.244 35.709 42.390 1.00 63.44 B C ATOM 1985 O ALA B 58 5.012 36.411 43.050 1.00 64.10 B O ATOM 1986 N GLY B 68 −0.478 27.631 40.155 1.00 63.44 B N ATOM 1987 CA GLY B 68 −1.756 28.210 39.773 1.00 62.59 B C ATOM 1988 C GLY B 68 −1.601 29.438 38.898 1.00 68.63 B C ATOM 1989 O GLY B 68 −1.904 29.392 37.704 1.00 70.46 B O ATOM 1990 N PRO B 69 −1.140 30.554 39.491 1.00 69.84 B N ATOM 1991 CD PRO B 69 −1.008 30.783 40.938 1.00 69.42 B C ATOM 1992 CA PRO B 69 −0.793 31.750 38.719 1.00 69.14 B C ATOM 1993 CB PRO B 69 −0.533 32.811 39.800 1.00 62.23 B C ATOM 1994 CG PRO B 69 −1.140 32.268 41.045 1.00 63.43 B C ATOM 1995 C PRO B 69 0.481 31.499 37.918 1.00 63.39 B C ATOM 1996 O PRO B 69 0.449 31.537 36.690 1.00 58.81 B O ATOM 1997 N ALA B 70 1.576 31.230 38.626 1.00 62.91 B N ATOM 1998 CA ALA B 70 2.873 30.931 38.022 1.00 58.68 B C ATOM 1999 CB ALA B 70 3.832 30.383 39.077 1.00 51.53 B C ATOM 2000 C ALA B 70 2.798 29.970 36.834 1.00 58.45 B C ATOM 2001 O ALA B 70 3.622 30.044 35.924 1.00 54.87 B O ATOM 2002 N LEU B 71 1.820 29.068 36.845 1.00 60.52 B N ATOM 2003 CA LEU B 71 1.701 28.070 35.783 1.00 59.07 B C ATOM 2004 CB LEU B 71 0.834 26.900 36.235 1.00 60.35 B C ATOM 2005 CG LEU B 71 1.654 25.740 36.788 1.00 67.52 B C ATOM 2006 CD1 LEU B 71 0.773 24.747 37.541 1.00 63.12 B C ATOM 2007 CD2 LEU B 71 2.439 25.057 35.670 1.00 56.79 B C ATOM 2008 C LEU B 71 1.176 28.631 34.466 1.00 62.30 B C ATOM 2009 O LEU B 71 1.462 28.094 33.397 1.00 58.91 B O ATOM 2010 N LEU B 72 0.396 29.702 34.541 1.00 65.72 B N ATOM 2011 CA LEU B 72 −0.087 30.341 33.331 1.00 61.97 B C ATOM 2012 CB LEU B 72 −1.323 31.192 33.622 1.00 57.06 B C ATOM 2013 CG LEU B 72 −2.488 30.872 32.689 1.00 58.07 B C ATOM 2014 CD1 LEU B 72 −3.810 31.205 33.337 1.00 64.14 B C ATOM 2015 CD2 LEU B 72 −2.426 29.408 32.343 1.00 62.65 B C ATOM 2016 C LEU B 72 1.051 31.175 32.771 1.00 58.95 B C ATOM 2017 O LEU B 72 1.229 31.276 31.556 1.00 63.17 B O ATOM 2018 N LEU B 73 1.839 31.744 33.675 1.00 51.63 B N ATOM 2019 CA LEU B 73 3.030 32.469 33.293 1.00 52.68 B C ATOM 2020 CB LEU B 73 3.800 32.887 34.538 1.00 52.13 B C ATOM 2021 CG LEU B 73 3.214 34.073 35.289 1.00 57.76 B C ATOM 2022 CD1 LEU B 73 4.083 34.435 36.485 1.00 56.21 B C ATOM 2023 CD2 LEU B 73 3.065 35.251 34.341 1.00 54.00 B C ATOM 2024 C LEU B 73 3.903 31.578 32.421 1.00 55.69 B C ATOM 2025 O LEU B 73 4.357 31.979 31.349 1.00 53.22 B O ATOM 2026 N LEU B 74 4.129 30.359 32.895 1.00 56.01 B N ATOM 2027 CA LEU B 74 4.998 29.419 32.209 1.00 56.68 B C ATOM 2028 CB LEU B 74 5.294 28.207 33.091 1.00 52.74 B C ATOM 2029 CG LEU B 74 5.912 27.025 32.347 1.00 52.55 B C ATOM 2030 CD1 LEU B 74 6.913 26.293 33.215 1.00 58.39 B C ATOM 2031 CD2 LEU B 74 4.832 26.084 31.855 1.00 53.12 B C ATOM 2032 C LEU B 74 4.408 28.967 30.890 1.00 55.52 B C ATOM 2033 O LEU B 74 5.138 28.647 29.959 1.00 58.29 B O ATOM 2034 N GLN B 75 3.084 28.935 30.816 1.00 58.82 B N ATOM 2035 CA GLN B 75 2.409 28.488 29.608 1.00 60.75 B C ATOM 2036 CB GLN B 75 1.036 27.911 29.953 1.00 64.75 B C ATOM 2037 CG GLN B 75 1.094 26.628 30.780 1.00 59.69 B C ATOM 2038 CD GLN B 75 −0.278 26.166 31.244 1.00 65.31 B C ATOM 2039 OE1 GLN B 75 −1.069 26.956 31.768 1.00 60.62 B O ATOM 2040 NE2 GLN B 75 −0.567 24.881 31.054 1.00 63.22 B N ATOM 2041 C GLN B 75 2.295 29.634 28.606 1.00 62.51 B C ATOM 2042 O GLN B 75 2.010 29.420 27.428 1.00 62.06 B O ATOM 2043 N LYS B 76 2.520 30.853 29.087 1.00 58.37 B N ATOM 2044 CA LYS B 76 2.634 32.010 28.213 1.00 60.04 B C ATOM 2045 CB LYS B 76 2.409 33.314 28.989 1.00 62.09 B C ATOM 2046 CG LYS B 76 0.952 33.643 29.276 1.00 60.25 B C ATOM 2047 CD LYS B 76 0.776 35.119 29.624 1.00 71.62 B C ATOM 2048 CE LYS B 76 −0.702 35.504 29.793 1.00 69.25 B C ATOM 2049 NZ LYS B 76 −1.297 34.977 31.054 1.00 59.05 B N ATOM 2050 C LYS B 76 4.016 32.020 27.560 1.00 60.31 B C ATOM 2051 O LYS B 76 4.131 32.040 26.334 1.00 56.69 B O ATOM 2052 N GLN B 77 5.058 32.002 28.391 1.00 58.08 B N ATOM 2053 CA GLN B 77 6.439 31.968 27.914 1.00 54.06 B C ATOM 2054 CB GLN B 77 7.419 31.724 29.069 1.00 59.51 B C ATOM 2055 CG GLN B 77 7.915 32.974 29.772 1.00 63.26 B C ATOM 2056 CD GLN B 77 8.706 33.893 28.859 1.00 63.95 B C ATOM 2057 OE1 GLN B 77 8.493 35.106 28.849 1.00 67.19 B O ATOM 2058 NE2 GLN B 77 9.623 33.319 28.084 1.00 60.61 B N ATOM 2059 C GLN B 77 6.653 30.890 26.865 1.00 53.18 B C ATOM 2060 O GLN B 77 7.160 31.166 25.789 1.00 56.68 B O ATOM 2061 N LEU B 78 6.277 29.657 27.186 1.00 52.31 B N ATOM 2062 CA LEU B 78 6.558 28.529 26.308 1.00 53.52 B C ATOM 2063 CB LEU B 78 6.668 27.235 27.115 1.00 56.76 B C ATOM 2064 CG LEU B 78 7.468 27.277 28.418 1.00 55.60 B C ATOM 2065 CD1 LEU B 78 7.738 25.865 28.916 1.00 53.16 B C ATOM 2066 CD2 LEU B 78 8.771 28.036 28.237 1.00 49.17 B C ATOM 2067 C LEU B 78 5.503 28.361 25.223 1.00 53.79 B C ATOM 2068 O LEU B 78 5.584 27.435 24.420 1.00 50.25 B O ATOM 2069 N SER B 79 4.517 29.256 25.204 1.00 58.17 B N ATOM 2070 CA SER B 79 3.403 29.156 24.262 1.00 54.14 B C ATOM 2071 CB SER B 79 3.870 29.384 22.824 1.00 49.92 B C ATOM 2072 OG SER B 79 3.766 30.752 22.486 1.00 48.45 B O ATOM 2073 C SER B 79 2.707 27.811 24.385 1.00 53.97 B C ATOM 2074 O SER B 79 2.625 27.041 23.421 1.00 50.65 B O ATOM 2075 N LEU B 80 2.216 27.539 25.591 1.00 60.28 B N ATOM 2076 CA LEU B 80 1.456 26.330 25.880 1.00 62.42 B C ATOM 2077 CB LEU B 80 2.010 25.649 27.131 1.00 58.16 B C ATOM 2078 CG LEU B 80 3.369 24.973 27.010 1.00 55.91 B C ATOM 2079 CD1 LEU B 80 3.724 24.297 28.322 1.00 57.99 B C ATOM 2080 CD2 LEU B 80 3.352 23.967 25.873 1.00 60.66 B C ATOM 2081 C LEU B 80 −0.006 26.687 26.114 1.00 57.37 B C ATOM 2082 O LEU B 80 −0.303 27.796 26.557 1.00 60.13 B O ATOM 2083 N PRO B 81 −0.922 25.750 25.814 1.00 61.97 B N ATOM 2084 CD PRO B 81 −0.686 24.474 25.111 1.00 61.25 B C ATOM 2085 CA PRO B 81 −2.330 25.909 26.189 1.00 60.47 B C ATOM 2086 CB PRO B 81 −2.847 24.472 26.167 1.00 57.27 B C ATOM 2087 CG PRO B 81 −2.064 23.831 25.078 1.00 48.71 B C ATOM 2088 C PRO B 81 −2.434 26.484 27.594 1.00 62.47 B C ATOM 2089 O PRO B 81 −2.095 25.797 28.562 1.00 61.09 B O ATOM 2090 N GLU B 82 −2.890 27.732 27.688 1.00 59.56 B N ATOM 2091 CA GLU B 82 −2.887 28.479 28.942 1.00 58.94 B C ATOM 2092 CB GLU B 82 −3.020 29.981 28.662 1.00 60.91 B C ATOM 2093 CG GLU B 82 −2.035 30.517 27.637 1.00 64.84 B C ATOM 2094 CD GLU B 82 −1.922 32.032 27.667 1.00 72.77 B C ATOM 2095 OE1 GLU B 82 −2.023 32.608 28.773 1.00 70.95 B O ATOM 2096 OE2 GLU B 82 −1.721 32.643 26.590 1.00 66.58 B O ATOM 2097 C GLU B 82 −3.989 28.019 29.901 1.00 62.99 B C ATOM 2098 O GLU B 82 −4.970 28.730 30.128 1.00 54.76 B O ATOM 2099 N THR B 83 −3.814 26.831 30.470 1.00 64.82 B N ATOM 2100 CA THR B 83 −4.801 26.272 31.383 1.00 63.98 B C ATOM 2101 CB THR B 83 −4.758 24.737 31.388 1.00 57.18 B C ATOM 2102 OG1 THR B 83 −3.444 24.298 31.739 1.00 60.21 B O ATOM 2103 CG2 THR B 83 −5.110 24.195 30.022 1.00 52.46 B C ATOM 2104 C THR B 83 −4.642 26.799 32.813 1.00 62.61 B C ATOM 2105 O THR B 83 −5.580 27.350 33.378 1.00 71.68 B O ATOM 2106 N GLY B 84 −3.454 26.641 33.386 1.00 62.09 B N ATOM 2107 CA GLY B 84 −3.214 26.994 34.778 1.00 60.11 B C ATOM 2108 C GLY B 84 −3.079 25.715 35.581 1.00 63.64 B C ATOM 2109 O GLY B 84 −2.949 25.725 36.804 1.00 60.72 B O ATOM 2110 N GLU B 85 −3.096 24.604 34.855 1.00 67.12 B N ATOM 2111 CA GLU B 85 −3.132 23.270 35.428 1.00 64.23 B C ATOM 2112 CB GLU B 85 −4.035 22.398 34.561 1.00 70.24 B C ATOM 2113 CG GLU B 85 −5.422 22.978 34.354 1.00 68.25 B C ATOM 2114 CD GLU B 85 −6.416 22.450 35.365 1.00 71.42 B C ATOM 2115 OE1 GLU B 85 −6.710 21.237 35.302 1.00 61.20 B O ATOM 2116 OE2 GLU B 85 −6.896 23.239 36.214 1.00 63.85 B O ATOM 2117 C GLU B 85 −1.747 22.635 35.509 1.00 67.75 B C ATOM 2118 O GLU B 85 −0.748 23.313 35.714 1.00 73.21 B O ATOM 2119 N LEU B 86 −1.698 21.321 35.341 1.00 67.78 B N ATOM 2120 CA LEU B 86 −0.445 20.580 35.385 1.00 71.96 B C ATOM 2121 CB LEU B 86 −0.131 20.158 36.820 1.00 72.41 B C ATOM 2122 CG LEU B 86 1.294 19.762 37.207 1.00 66.28 B C ATOM 2123 CD1 LEU B 86 2.309 20.531 36.383 1.00 68.71 B C ATOM 2124 CD2 LEU B 86 1.495 18.272 37.056 1.00 72.56 B C ATOM 2125 C LEU B 86 −0.640 19.379 34.477 1.00 71.46 B C ATOM 2126 O LEU B 86 −0.585 18.227 34.908 1.00 74.91 B O ATOM 2127 N ASP B 87 −0.860 19.684 33.204 1.00 70.75 B N ATOM 2128 CA ASP B 87 −1.421 18.751 32.237 1.00 68.01 B C ATOM 2129 CB ASP B 87 −2.387 19.523 31.344 1.00 72.56 B C ATOM 2130 CG ASP B 87 −2.110 21.018 31.358 1.00 70.64 B C ATOM 2131 OD1 ASP B 87 −1.054 21.436 30.836 1.00 73.81 B O ATOM 2132 OD2 ASP B 87 −2.940 21.774 31.902 1.00 65.94 B O ATOM 2133 C ASP B 87 −0.397 18.013 31.378 1.00 71.38 B C ATOM 2134 O ASP B 87 0.804 18.265 31.460 1.00 73.55 B O ATOM 2135 N SER B 88 −0.895 17.101 30.547 1.00 71.40 B N ATOM 2136 CA SER B 88 −0.058 16.322 29.638 1.00 76.17 B C ATOM 2137 CB SER B 88 −0.914 15.285 28.901 1.00 81.14 B C ATOM 2138 OG SER B 88 −0.200 14.680 27.836 1.00 97.89 B O ATOM 2139 C SER B 88 0.682 17.211 28.634 1.00 76.49 B C ATOM 2140 O SER B 88 1.407 16.724 27.756 1.00 71.22 B O ATOM 2141 N ALA B 89 0.483 18.518 28.763 1.00 73.00 B N ATOM 2142 CA ALA B 89 1.181 19.488 27.937 1.00 67.00 B C ATOM 2143 CB ALA B 89 0.220 20.561 27.450 1.00 66.96 B C ATOM 2144 C ALA B 89 2.306 20.106 28.757 1.00 65.13 B C ATOM 2145 O ALA B 89 3.464 20.100 28.343 1.00 70.19 B O ATOM 2146 N THR B 90 1.958 20.624 29.928 1.00 62.06 B N ATOM 2147 CA THR B 90 2.939 21.232 30.813 1.00 61.02 B C ATOM 2148 CB THR B 90 2.265 22.093 31.904 1.00 60.52 B C ATOM 2149 OG1 THR B 90 1.360 23.020 31.295 1.00 54.25 B O ATOM 2150 CG2 THR B 90 3.301 22.870 32.691 1.00 58.17 B C ATOM 2151 C THR B 90 3.824 20.168 31.461 1.00 65.81 B C ATOM 2152 O THR B 90 4.880 20.478 32.010 1.00 65.96 B O ATOM 2153 N LEU B 91 3.397 18.910 31.392 1.00 67.51 B N ATOM 2154 CA LEU B 91 4.199 17.810 31.924 1.00 68.60 B C ATOM 2155 CB LEU B 91 3.320 16.618 32.297 1.00 72.84 B C ATOM 2156 CG LEU B 91 2.967 16.597 33.781 1.00 70.90 B C ATOM 2157 CD1 LEU B 91 2.895 18.017 34.272 1.00 67.17 B C ATOM 2158 CD2 LEU B 91 1.663 15.854 34.042 1.00 74.75 B C ATOM 2159 C LEU B 91 5.283 17.391 30.944 1.00 64.01 B C ATOM 2160 O LEU B 91 6.462 17.305 31.299 1.00 58.07 B O ATOM 2161 N LYS B 92 4.882 17.125 29.708 1.00 62.63 B N ATOM 2162 CA LYS B 92 5.862 16.914 28.663 1.00 66.15 B C ATOM 2163 CB LYS B 92 5.198 16.788 27.292 1.00 64.51 B C ATOM 2164 CG LYS B 92 6.167 16.403 26.186 1.00 61.84 B C ATOM 2165 CD LYS B 92 5.496 16.412 24.824 1.00 67.85 B C ATOM 2166 CE LYS B 92 6.528 16.500 23.711 1.00 68.24 B C ATOM 2167 NZ LYS B 92 7.446 17.660 23.914 1.00 70.30 B N ATOM 2168 C LYS B 92 6.808 18.108 28.696 1.00 63.81 B C ATOM 2169 O LYS B 92 7.995 17.954 28.967 1.00 63.68 B O ATOM 2170 N ALA B 93 6.267 19.299 28.453 1.00 56.96 B N ATOM 2171 CA ALA B 93 7.060 20.521 28.450 1.00 51.81 B C ATOM 2172 CB ALA B 93 6.152 21.733 28.527 1.00 51.49 B C ATOM 2173 C ALA B 93 8.098 20.551 29.576 1.00 57.02 B C ATOM 2174 O ALA B 93 9.286 20.784 29.336 1.00 61.50 B O ATOM 2175 N MET B 94 7.652 20.303 30.801 1.00 59.70 B N ATOM 2176 CA MET B 94 8.541 20.336 31.960 1.00 58.29 B C ATOM 2177 CB MET B 94 7.732 20.324 33.261 1.00 60.51 B C ATOM 2178 CG MET B 94 7.272 21.705 33.733 1.00 62.85 B C ATOM 2179 SD MET B 94 5.978 21.641 35.001 1.00 55.45 B S ATOM 2180 CE MET B 94 6.094 23.278 35.712 1.00 53.95 B C ATOM 2181 C MET B 94 9.591 19.217 31.965 1.00 62.12 B C ATOM 2182 O MET B 94 10.606 19.317 32.654 1.00 63.47 B O ATOM 2183 N ARG B 95 9.351 18.160 31.195 1.00 61.52 B N ATOM 2184 CA ARG B 95 10.307 17.059 31.091 1.00 56.19 B C ATOM 2185 CB ARG B 95 9.586 15.726 30.881 1.00 66.06 B C ATOM 2186 CG ARG B 95 8.885 15.178 32.097 1.00 65.13 B C ATOM 2187 CD ARG B 95 8.530 13.723 31.881 1.00 63.53 B C ATOM 2188 NE ARG B 95 7.270 13.378 32.528 1.00 70.76 B N ATOM 2189 CZ ARG B 95 6.114 13.271 31.883 1.00 72.75 B C ATOM 2190 NH1 ARG B 95 6.068 13.472 30.572 1.00 73.16 B N ATOM 2191 NH2 ARG B 95 5.008 12.958 32.545 1.00 67.06 B N ATOM 2192 C ARG B 95 11.284 17.244 29.942 1.00 53.67 B C ATOM 2193 O ARG B 95 12.251 16.488 29.817 1.00 50.81 B O ATOM 2194 N THR B 96 11.024 18.225 29.086 1.00 51.50 B N ATOM 2195 CA THR B 96 11.842 18.394 27.895 1.00 48.95 B C ATOM 2196 CB THR B 96 11.091 19.137 26.779 1.00 49.75 B C ATOM 2197 OG1 THR B 96 9.904 18.410 26.441 1.00 59.02 B O ATOM 2198 CG2 THR B 96 11.956 19.241 25.541 1.00 43.36 B C ATOM 2199 C THR B 96 13.145 19.104 28.224 1.00 48.58 B C ATOM 2200 O THR B 96 13.134 20.179 28.826 1.00 52.86 B O ATOM 2201 N PRO B 97 14.275 18.485 27.843 1.00 53.45 B N ATOM 2202 CD PRO B 97 14.299 17.154 27.216 1.00 50.12 B C ATOM 2203 CA PRO B 97 15.629 19.032 27.989 1.00 48.45 B C ATOM 2204 CB PRO B 97 16.443 18.165 27.046 1.00 45.26 B C ATOM 2205 CG PRO B 97 15.766 16.850 27.128 1.00 49.95 B C ATOM 2206 C PRO B 97 15.673 20.486 27.559 1.00 45.10 B C ATOM 2207 O PRO B 97 15.021 20.879 26.597 1.00 47.02 B O ATOM 2208 N ARG B 98 16.454 21.275 28.274 1.00 41.15 B N ATOM 2209 CA ARG B 98 16.255 22.700 28.259 1.00 39.57 B C ATOM 2210 CB ARG B 98 15.497 23.070 29.526 1.00 40.45 B C ATOM 2211 CG ARG B 98 14.288 23.919 29.304 1.00 48.97 B C ATOM 2212 CD ARG B 98 13.820 24.504 30.613 1.00 41.86 B C ATOM 2213 NE ARG B 98 14.341 25.851 30.795 1.00 42.00 B N ATOM 2214 CZ ARG B 98 13.643 26.952 30.547 1.00 44.30 B C ATOM 2215 NH1 ARG B 98 12.389 26.861 30.116 1.00 36.29 B N ATOM 2216 NH2 ARG B 98 14.198 28.142 30.737 1.00 43.05 B N ATOM 2217 C ARG B 98 17.575 23.445 28.288 1.00 45.87 B C ATOM 2218 O ARG B 98 18.639 22.871 28.546 1.00 41.37 B O ATOM 2219 N CYS B 99 17.490 24.744 28.043 1.00 41.10 B N ATOM 2220 CA CYS B 99 18.580 25.638 28.369 1.00 39.89 B C ATOM 2221 CB CYS B 99 18.547 26.865 27.469 1.00 35.02 B C ATOM 2222 SG CYS B 99 19.709 28.100 28.000 1.00 35.66 B S ATOM 2223 C CYS B 99 18.451 26.064 29.839 1.00 46.12 B C ATOM 2224 O CYS B 99 17.344 26.215 30.354 1.00 37.35 B O ATOM 2225 N GLY B 100 19.584 26.260 30.509 1.00 43.34 B N ATOM 2226 CA GLY B 100 19.579 26.584 31.921 1.00 40.75 B C ATOM 2227 C GLY B 100 19.165 28.007 32.236 1.00 40.76 B C ATOM 2228 O GLY B 100 18.657 28.297 33.320 1.00 41.17 B O ATOM 2229 N VAL B 101 19.387 28.908 31.290 1.00 42.65 B N ATOM 2230 CA VAL B 101 19.087 30.311 31.533 1.00 47.46 B C ATOM 2231 CB VAL B 101 19.552 31.197 30.352 1.00 39.84 B C ATOM 2232 CG1 VAL B 101 18.937 32.582 30.425 1.00 40.45 B C ATOM 2233 CG2 VAL B 101 21.059 31.287 30.338 1.00 36.80 B C ATOM 2234 C VAL B 101 17.600 30.494 31.832 1.00 42.44 B C ATOM 2235 O VAL B 101 16.759 29.986 31.105 1.00 46.63 B O ATOM 2236 N PRO B 102 17.278 31.198 32.927 1.00 44.08 B N ATOM 2237 CA PRO B 102 15.889 31.462 33.333 1.00 46.95 B C ATOM 2238 C PRO B 102 15.091 32.224 32.279 1.00 46.22 B C ATOM 2239 CB PRO B 102 16.049 32.306 34.602 1.00 49.61 B C ATOM 2240 CG PRO B 102 17.386 31.905 35.150 1.00 48.94 B C ATOM 2241 CD PRO B 102 18.246 31.660 33.936 1.00 47.68 B C ATOM 2242 O PRO B 102 15.682 32.891 31.428 1.00 43.88 B O ATOM 2243 N ASP B 103 13.764 32.118 32.342 1.00 45.75 B N ATOM 2244 CA ASP B 103 12.877 32.721 31.348 1.00 42.66 B C ATOM 2245 C ASP B 103 12.351 34.085 31.790 1.00 46.42 B C ATOM 2246 CB ASP B 103 11.708 31.787 31.039 1.00 43.94 B C ATOM 2247 CG ASP B 103 12.163 30.413 30.580 1.00 47.78 B C ATOM 2248 OD1 ASP B 103 13.226 30.331 29.932 1.00 43.44 B O ATOM 2249 OD2 ASP B 103 11.457 29.416 30.860 1.00 48.02 B O ATOM 2250 O ASP B 103 12.030 34.929 30.958 1.00 48.95 B O ATOM 2251 N LEU B 104 12.251 34.291 33.100 1.00 56.26 B N ATOM 2252 CA LEU B 104 11.881 35.594 33.656 1.00 54.57 B C ATOM 2253 C LEU B 104 12.873 35.926 34.754 1.00 62.42 B C ATOM 2254 CB LEU B 104 10.467 35.573 34.233 1.00 54.89 B C ATOM 2255 CG LEU B 104 9.386 34.777 33.493 1.00 59.53 B C ATOM 2256 CD1 LEU B 104 8.117 34.686 34.334 1.00 56.01 B C ATOM 2257 CD2 LEU B 104 9.097 35.378 32.125 1.00 53.55 B C ATOM 2258 O LEU B 104 12.626 35.647 35.929 1.00 71.10 B O ATOM 2259 N GLY B 105 13.994 36.528 34.364 1.00 70.21 B N ATOM 2260 CA GLY B 105 15.141 36.659 35.243 1.00 73.75 B C ATOM 2261 C GLY B 105 15.345 37.991 35.935 1.00 73.86 B C ATOM 2262 O GLY B 105 15.215 39.052 35.327 1.00 80.83 B O ATOM 2263 N ARG B 106 15.665 37.910 37.224 1.00 79.69 B N ATOM 2264 CA ARG B 106 16.064 39.047 38.049 1.00 74.60 B C ATOM 2265 C ARG B 106 17.383 39.606 37.527 1.00 82.15 B C ATOM 2266 CB ARG B 106 16.256 38.570 39.488 1.00 79.05 B C ATOM 2267 CG ARG B 106 17.196 37.361 39.621 1.00 76.81 B C ATOM 2268 CD ARG B 106 16.514 36.053 39.219 1.00 75.56 B C ATOM 2269 NE ARG B 106 17.464 34.954 39.059 1.00 79.25 B N ATOM 2270 CZ ARG B 106 17.115 33.679 38.897 1.00 76.89 B C ATOM 2271 NH1 ARG B 106 15.830 33.339 38.877 1.00 69.62 B N ATOM 2272 NH2 ARG B 106 18.050 32.743 38.759 1.00 62.05 B N ATOM 2273 O ARG B 106 18.369 39.699 38.268 1.00 80.20 B O ATOM 2274 N PHE B 107 17.378 40.008 36.257 1.00 85.16 B N ATOM 2275 CA PHE B 107 18.598 40.054 35.439 1.00 78.48 B C ATOM 2276 C PHE B 107 19.871 40.672 36.031 1.00 76.74 B C ATOM 2277 CB PHE B 107 18.331 40.533 33.992 1.00 75.03 B C ATOM 2278 CG PHE B 107 17.627 41.860 33.879 1.00 83.31 B C ATOM 2279 CD1 PHE B 107 16.272 41.978 34.168 1.00 82.00 B C ATOM 2280 CD2 PHE B 107 18.310 42.980 33.421 1.00 79.46 B C ATOM 2281 CE1 PHE B 107 15.622 43.197 34.041 1.00 81.08 B C ATOM 2282 CE2 PHE B 107 17.667 44.201 33.290 1.00 79.56 B C ATOM 2283 CZ PHE B 107 16.320 44.309 33.601 1.00 82.34 B C ATOM 2284 O PHE B 107 20.819 39.939 36.318 1.00 69.47 B O ATOM 2285 N GLN B 108 19.895 41.991 36.214 1.00 79.36 B N ATOM 2286 CA GLN B 108 21.153 42.696 36.495 1.00 71.01 B C ATOM 2287 C GLN B 108 21.945 42.287 37.756 1.00 72.52 B C ATOM 2288 CB GLN B 108 20.990 44.218 36.376 1.00 70.87 B C ATOM 2289 CG GLN B 108 21.307 44.738 34.968 1.00 73.74 B C ATOM 2290 CD GLN B 108 21.063 46.232 34.809 1.00 77.39 B C ATOM 2291 OE1 GLN B 108 20.028 46.755 35.235 1.00 71.06 B O ATOM 2292 NE2 GLN B 108 22.012 46.923 34.181 1.00 60.71 B N ATOM 2293 O GLN B 108 22.634 43.106 38.368 1.00 69.21 B O ATOM 2294 N VAL B 109 21.852 41.007 38.115 1.00 71.72 B N ATOM 2295 CA VAL B 109 22.927 40.317 38.813 1.00 65.27 B C ATOM 2296 C VAL B 109 24.170 40.545 37.951 1.00 60.53 B C ATOM 2297 CB VAL B 109 22.644 38.788 38.874 1.00 72.89 B C ATOM 2298 CG1 VAL B 109 21.320 38.503 39.577 1.00 73.16 B C ATOM 2299 CG2 VAL B 109 23.797 38.023 39.533 1.00 68.50 B C ATOM 2300 O VAL B 109 25.255 40.043 38.237 1.00 57.47 B O ATOM 2301 N PHE B 110 23.982 41.312 36.879 1.00 63.50 B N ATOM 2302 CA PHE B 110 24.991 41.522 35.850 1.00 57.69 B C ATOM 2303 C PHE B 110 25.415 42.977 35.719 1.00 51.67 B C ATOM 2304 CB PHE B 110 24.465 41.024 34.509 1.00 49.06 B C ATOM 2305 CG PHE B 110 24.123 39.571 34.510 1.00 54.61 B C ATOM 2306 CD1 PHE B 110 25.062 38.631 34.895 1.00 52.85 B C ATOM 2307 CD2 PHE B 110 22.868 39.141 34.130 1.00 57.14 B C ATOM 2308 CE1 PHE B 110 24.761 37.293 34.899 1.00 53.90 B C ATOM 2309 CE2 PHE B 110 22.558 37.800 34.137 1.00 58.98 B C ATOM 2310 CZ PHE B 110 23.506 36.874 34.522 1.00 58.60 B C ATOM 2311 O PHE B 110 24.600 43.894 35.826 1.00 55.38 B O ATOM 2312 N GLU B 111 26.701 43.176 35.468 1.00 50.32 B N ATOM 2313 CA GLU B 111 27.252 44.512 35.308 1.00 51.37 B C ATOM 2314 CB GLU B 111 28.754 44.500 35.595 1.00 50.26 B C ATOM 2315 CG GLU B 111 29.351 45.870 35.892 1.00 61.59 B C ATOM 2316 CD GLU B 111 30.847 45.806 36.182 1.00 70.62 B C ATOM 2317 OE1 GLU B 111 31.246 45.021 37.074 1.00 63.54 B O ATOM 2318 OE2 GLU B 111 31.619 46.543 35.518 1.00 61.97 B O ATOM 2319 C GLU B 111 26.976 45.074 33.913 1.00 48.33 B C ATOM 2320 O GLU B 111 26.871 44.337 32.935 1.00 46.73 B O ATOM 2321 N GLY B 112 26.814 46.387 33.840 1.00 51.87 B N ATOM 2322 CA GLY B 112 26.801 47.074 32.565 1.00 55.06 B C ATOM 2323 C GLY B 112 25.555 46.978 31.710 1.00 56.42 B C ATOM 2324 O GLY B 112 24.436 46.826 32.198 1.00 49.39 B O ATOM 2325 N ASP B 113 25.776 47.057 30.404 1.00 58.88 B N ATOM 2326 CA ASP B 113 24.714 47.287 29.433 1.00 56.55 B C ATOM 2327 CB ASP B 113 25.290 48.105 28.280 1.00 46.86 B C ATOM 2328 CG ASP B 113 24.233 48.780 27.477 1.00 51.13 B C ATOM 2329 OD1 ASP B 113 23.112 48.940 28.001 1.00 53.14 B O ATOM 2330 OD2 ASP B 113 24.525 49.155 26.326 1.00 64.56 B O ATOM 2331 C ASP B 113 24.069 45.999 28.898 1.00 53.37 B C ATOM 2332 O ASP B 113 22.924 46.010 28.431 1.00 49.47 B O ATOM 2333 N LEU B 114 24.816 44.899 28.966 1.00 47.53 B N ATOM 2334 CA LEU B 114 24.363 43.603 28.461 1.00 47.15 B C ATOM 2335 CB LEU B 114 23.022 43.206 29.080 1.00 46.85 B C ATOM 2336 CG LEU B 114 22.996 43.324 30.608 1.00 50.33 B C ATOM 2337 CD1 LEU B 114 21.901 42.462 31.207 1.00 48.76 B C ATOM 2338 CD2 LEU B 114 24.353 42.956 31.203 1.00 48.21 B C ATOM 2339 C LEU B 114 24.317 43.578 26.928 1.00 51.92 B C ATOM 2340 O LEU B 114 23.498 42.882 26.322 1.00 50.80 B O ATOM 2341 N LYS B 115 25.210 44.366 26.331 1.00 52.50 B N ATOM 2342 CA LYS B 115 25.484 44.390 24.900 1.00 46.97 B C ATOM 2343 CB LYS B 115 24.905 45.649 24.257 1.00 48.03 B C ATOM 2344 CG LYS B 115 23.455 45.569 23.842 1.00 49.71 B C ATOM 2345 CD LYS B 115 22.921 46.969 23.559 1.00 58.89 B C ATOM 2346 CE LYS B 115 23.887 47.787 22.699 1.00 56.85 B C ATOM 2347 NZ LYS B 115 23.534 47.781 21.249 1.00 43.43 B N ATOM 2348 C LYS B 115 26.996 44.444 24.741 1.00 48.75 B C ATOM 2349 O LYS B 115 27.725 44.707 25.709 1.00 48.65 B O ATOM 2350 N TRP B 116 27.474 44.211 23.526 1.00 42.34 B N ATOM 2351 CA TRP B 116 28.878 44.453 23.241 1.00 43.79 B C ATOM 2352 CB TRP B 116 29.413 43.443 22.235 1.00 44.73 B C ATOM 2353 CG TRP B 116 29.479 42.030 22.741 1.00 44.36 B C ATOM 2354 CD2 TRP B 116 30.218 41.542 23.874 1.00 39.82 B C ATOM 2355 CE2 TRP B 116 29.988 40.158 23.955 1.00 39.86 B C ATOM 2356 CE3 TRP B 116 31.047 42.141 24.822 1.00 41.32 B C ATOM 2357 CD1 TRP B 116 28.856 40.950 22.202 1.00 42.85 B C ATOM 2358 NE1 TRP B 116 29.153 39.824 22.923 1.00 50.04 B N ATOM 2359 CZ2 TRP B 116 30.553 39.361 24.945 1.00 38.59 B C ATOM 2360 CZ3 TRP B 116 31.601 41.351 25.808 1.00 45.80 B C ATOM 2361 CH2 TRP B 116 31.351 39.973 25.864 1.00 42.53 B C ATOM 2362 C TRP B 116 29.059 45.873 22.715 1.00 42.44 B C ATOM 2363 O TRP B 116 28.190 46.403 22.029 1.00 41.43 B O ATOM 2364 N HIS B 117 30.182 46.498 23.038 1.00 44.50 B N ATOM 2365 CA HIS B 117 30.439 47.843 22.534 1.00 47.40 B C ATOM 2366 CB HIS B 117 30.401 48.863 23.670 1.00 47.30 B C ATOM 2367 CG HIS B 117 29.047 49.001 24.293 1.00 50.75 B C ATOM 2368 CD2 HIS B 117 27.949 49.691 23.898 1.00 54.32 B C ATOM 2369 ND1 HIS B 117 28.688 48.345 25.452 1.00 53.55 B N ATOM 2370 CE1 HIS B 117 27.433 48.636 25.753 1.00 51.35 B C ATOM 2371 NE2 HIS B 117 26.961 49.451 24.826 1.00 55.23 B N ATOM 2372 C HIS B 117 31.723 47.931 21.707 1.00 51.10 B C ATOM 2373 O HIS B 117 32.396 48.963 21.681 1.00 54.55 B O ATOM 2374 N HIS B 118 32.037 46.822 21.039 1.00 45.47 B N ATOM 2375 CA HIS B 118 33.109 46.737 20.053 1.00 53.46 B C ATOM 2376 CB HIS B 118 34.444 46.420 20.714 1.00 49.44 B C ATOM 2377 CG HIS B 118 34.449 45.125 21.461 1.00 50.04 B C ATOM 2378 CD2 HIS B 118 34.854 43.888 21.096 1.00 48.01 B C ATOM 2379 ND1 HIS B 118 33.980 45.014 22.753 1.00 49.91 B N ATOM 2380 CE1 HIS B 118 34.105 43.761 23.154 1.00 51.40 B C ATOM 2381 NE2 HIS B 118 34.633 43.058 22.169 1.00 51.26 B N ATOM 2382 C HIS B 118 32.714 45.621 19.096 1.00 50.28 B C ATOM 2383 O HIS B 118 32.017 44.696 19.491 1.00 46.97 B O ATOM 2384 N HIS B 119 33.145 45.706 17.843 1.00 47.92 B N ATOM 2385 CA HIS B 119 32.567 44.860 16.800 1.00 49.38 B C ATOM 2386 CB HIS B 119 32.604 45.570 15.449 1.00 47.66 B C ATOM 2387 CG HIS B 119 33.991 45.830 14.947 1.00 66.83 B C ATOM 2388 CD2 HIS B 119 34.861 46.841 15.203 1.00 63.36 B C ATOM 2389 ND1 HIS B 119 34.642 44.983 14.073 1.00 65.14 B N ATOM 2390 CE1 HIS B 119 35.845 45.461 13.809 1.00 62.80 B C ATOM 2391 NE2 HIS B 119 36.000 46.590 14.481 1.00 64.56 B N ATOM 2392 C HIS B 119 33.227 43.493 16.680 1.00 48.74 B C ATOM 2393 O HIS B 119 32.591 42.526 16.271 1.00 46.40 B O ATOM 2394 N ASN B 120 34.505 43.411 17.019 1.00 53.45 B N ATOM 2395 CA ASN B 120 35.214 42.148 16.877 1.00 49.60 B C ATOM 2396 CB ASN B 120 36.614 42.353 16.299 1.00 44.14 B C ATOM 2397 CG ASN B 120 37.462 41.099 16.390 1.00 51.69 B C ATOM 2398 OD1 ASN B 120 37.046 40.011 15.969 1.00 45.02 B O ATOM 2399 ND2 ASN B 120 38.656 41.239 16.954 1.00 50.93 B N ATOM 2400 C ASN B 120 35.287 41.396 18.195 1.00 49.18 B C ATOM 2401 O ASN B 120 36.098 41.714 19.066 1.00 45.24 B O ATOM 2402 N ILE B 121 34.433 40.388 18.326 1.00 50.38 B N ATOM 2403 CA ILE B 121 34.361 39.597 19.544 1.00 49.52 B C ATOM 2404 CB ILE B 121 32.955 39.068 19.757 1.00 39.76 B C ATOM 2405 CG2 ILE B 121 32.875 38.327 21.063 1.00 43.00 B C ATOM 2406 CG1 ILE B 121 31.965 40.230 19.706 1.00 44.80 B C ATOM 2407 CD1 ILE B 121 32.426 41.441 20.466 1.00 45.45 B C ATOM 2408 C ILE B 121 35.325 38.423 19.509 1.00 43.32 B C ATOM 2409 O ILE B 121 35.358 37.664 18.545 1.00 45.27 B O ATOM 2410 N THR B 122 36.117 38.285 20.562 1.00 39.28 B N ATOM 2411 CA THR B 122 37.082 37.202 20.643 1.00 41.93 B C ATOM 2412 CB THR B 122 38.419 37.683 21.235 1.00 46.81 B C ATOM 2413 OG1 THR B 122 38.216 38.142 22.577 1.00 43.28 B O ATOM 2414 CG2 THR B 122 39.002 38.820 20.387 1.00 39.61 B C ATOM 2415 C THR B 122 36.499 36.109 21.510 1.00 42.10 B C ATOM 2416 O THR B 122 35.655 36.383 22.358 1.00 45.35 B O ATOM 2417 N TYR B 123 36.929 34.872 21.285 1.00 43.44 B N ATOM 2418 CA TYR B 123 36.443 33.739 22.070 1.00 39.13 B C ATOM 2419 CB TYR B 123 35.156 33.165 21.475 1.00 36.63 B C ATOM 2420 CG TYR B 123 35.285 32.416 20.163 1.00 36.92 B C ATOM 2421 CD1 TYR B 123 35.097 33.065 18.954 1.00 39.72 B C ATOM 2422 CE1 TYR B 123 35.175 32.388 17.754 1.00 38.16 B C ATOM 2423 CD2 TYR B 123 35.540 31.050 20.134 1.00 40.99 B C ATOM 2424 CE2 TYR B 123 35.625 30.358 18.935 1.00 34.84 B C ATOM 2425 CZ TYR B 123 35.438 31.037 17.747 1.00 42.37 B C ATOM 2426 OH TYR B 123 35.517 30.376 16.539 1.00 42.40 B O ATOM 2427 C TYR B 123 37.484 32.642 22.282 1.00 38.07 B C ATOM 2428 O TYR B 123 38.281 32.343 21.398 1.00 39.06 B O ATOM 2429 N TRP B 124 37.455 32.039 23.464 1.00 40.32 B N ATOM 2430 CA TRP B 124 38.491 31.109 23.883 1.00 40.84 B C ATOM 2431 CB TRP B 124 39.135 31.638 25.154 1.00 43.55 B C ATOM 2432 CG TRP B 124 40.249 30.805 25.670 1.00 46.76 B C ATOM 2433 CD2 TRP B 124 40.619 30.633 27.043 1.00 49.46 B C ATOM 2434 CE2 TRP B 124 41.751 29.790 27.067 1.00 53.85 B C ATOM 2435 CE3 TRP B 124 40.105 31.112 28.256 1.00 44.96 B C ATOM 2436 CD1 TRP B 124 41.149 30.088 24.935 1.00 44.04 B C ATOM 2437 NE1 TRP B 124 42.052 29.471 25.766 1.00 49.43 B N ATOM 2438 CZ2 TRP B 124 42.375 29.408 28.259 1.00 47.46 B C ATOM 2439 CZ3 TRP B 124 40.725 30.734 29.440 1.00 45.40 B C ATOM 2440 CH2 TRP B 124 41.848 29.891 29.431 1.00 55.02 B C ATOM 2441 C TRP B 124 37.954 29.719 24.153 1.00 41.37 B C ATOM 2442 O TRP B 124 37.390 29.471 25.209 1.00 53.15 B O ATOM 2443 N ILE B 125 38.123 28.808 23.208 1.00 37.64 B N ATOM 2444 CA ILE B 125 37.677 27.436 23.413 1.00 42.10 B C ATOM 2445 CB ILE B 125 37.799 26.613 22.124 1.00 46.72 B C ATOM 2446 CG2 ILE B 125 37.527 25.152 22.408 1.00 50.80 B C ATOM 2447 CG1 ILE B 125 36.837 27.155 21.059 1.00 46.91 B C ATOM 2448 CD1 ILE B 125 36.800 26.334 19.785 1.00 42.20 B C ATOM 2449 C ILE B 125 38.513 26.796 24.515 1.00 45.32 B C ATOM 2450 O ILE B 125 39.501 26.122 24.252 1.00 53.04 B O ATOM 2451 N GLN B 126 38.107 27.014 25.755 1.00 43.61 B N ATOM 2452 CA GLN B 126 38.965 26.747 26.903 1.00 45.07 B C ATOM 2453 CB GLN B 126 38.377 27.419 28.139 1.00 47.23 B C ATOM 2454 CG GLN B 126 39.255 27.384 29.366 1.00 46.29 B C ATOM 2455 CD GLN B 126 38.492 27.801 30.602 1.00 52.87 B C ATOM 2456 OE1 GLN B 126 37.382 27.318 30.861 1.00 52.66 B O ATOM 2457 NE2 GLN B 126 39.074 28.712 31.371 1.00 55.44 B N ATOM 2458 C GLN B 126 39.223 25.266 27.181 1.00 42.21 B C ATOM 2459 O GLN B 126 40.264 24.910 27.723 1.00 36.42 B O ATOM 2460 N ASN B 127 38.274 24.403 26.842 1.00 39.73 B N ATOM 2461 CA ASN B 127 38.502 22.965 26.981 1.00 46.07 B C ATOM 2462 CB ASN B 127 38.485 22.511 28.452 1.00 44.50 B C ATOM 2463 CG ASN B 127 37.132 22.690 29.110 1.00 46.02 B C ATOM 2464 OD1 ASN B 127 36.186 23.174 28.496 1.00 47.88 B O ATOM 2465 ND2 ASN B 127 37.038 22.298 30.369 1.00 51.76 B N ATOM 2466 C ASN B 127 37.548 22.148 26.125 1.00 43.66 B C ATOM 2467 O ASN B 127 36.642 22.702 25.515 1.00 42.64 B O ATOM 2468 N TYR B 128 37.767 20.837 26.071 1.00 42.86 B N ATOM 2469 CA TYR B 128 37.028 19.986 25.147 1.00 46.13 B C ATOM 2470 CB TYR B 128 37.914 19.550 23.988 1.00 42.01 B C ATOM 2471 CG TYR B 128 38.421 20.682 23.128 1.00 50.36 B C ATOM 2472 CD1 TYR B 128 37.748 21.049 21.972 1.00 47.28 B C ATOM 2473 CE1 TYR B 128 38.212 22.073 21.174 1.00 50.13 B C ATOM 2474 CD2 TYR B 128 39.586 21.374 23.462 1.00 52.15 B C ATOM 2475 CE2 TYR B 128 40.058 22.405 22.669 1.00 45.44 B C ATOM 2476 CZ TYR B 128 39.366 22.746 21.525 1.00 50.69 B C ATOM 2477 OH TYR B 128 39.813 23.769 20.726 1.00 55.45 B O ATOM 2478 C TYR B 128 36.451 18.748 25.803 1.00 54.02 B C ATOM 2479 O TYR B 128 37.048 18.173 26.713 1.00 57.00 B O ATOM 2480 N SER B 129 35.280 18.344 25.323 1.00 50.31 B N ATOM 2481 CA SER B 129 34.659 17.109 25.750 1.00 44.78 B C ATOM 2482 CB SER B 129 33.151 17.177 25.503 1.00 45.36 B C ATOM 2483 OG SER B 129 32.534 15.926 25.728 1.00 47.57 B O ATOM 2484 C SER B 129 35.289 15.980 24.952 1.00 43.51 B C ATOM 2485 O SER B 129 35.735 16.195 23.832 1.00 50.04 B O ATOM 2486 N GLU B 130 35.335 14.783 25.523 1.00 46.45 B N ATOM 2487 CA GLU B 130 35.942 13.645 24.842 1.00 48.02 B C ATOM 2488 CB GLU B 130 36.402 12.583 25.844 1.00 49.45 B C ATOM 2489 CG GLU B 130 37.648 12.964 26.619 1.00 56.40 B C ATOM 2490 CD GLU B 130 38.811 13.347 25.715 1.00 61.77 B C ATOM 2491 OE1 GLU B 130 39.200 12.527 24.858 1.00 71.84 B O ATOM 2492 OE2 GLU B 130 39.345 14.466 25.866 1.00 63.98 B O ATOM 2493 C GLU B 130 34.974 13.031 23.849 1.00 48.91 B C ATOM 2494 O GLU B 130 35.306 12.069 23.149 1.00 46.50 B O ATOM 2495 N ASP B 131 33.779 13.606 23.784 1.00 48.79 B N ATOM 2496 CA ASP B 131 32.689 13.028 23.010 1.00 49.17 B C ATOM 2497 CB ASP B 131 31.362 13.630 23.447 1.00 48.20 B C ATOM 2498 CG ASP B 131 30.926 13.123 24.799 1.00 54.48 B C ATOM 2499 OD1 ASP B 131 31.708 12.363 25.418 1.00 56.14 B O ATOM 2500 OD2 ASP B 131 29.807 13.476 25.236 1.00 52.94 B O ATOM 2501 C ASP B 131 32.865 13.180 21.511 1.00 53.98 B C ATOM 2502 O ASP B 131 32.403 12.333 20.742 1.00 56.76 B O ATOM 2503 N LEU B 132 33.523 14.264 21.105 1.00 51.78 B N ATOM 2504 CA LEU B 132 33.791 14.529 19.698 1.00 43.52 B C ATOM 2505 CB LEU B 132 32.954 15.708 19.207 1.00 43.67 B C ATOM 2506 CG LEU B 132 31.424 15.678 19.209 1.00 39.43 B C ATOM 2507 CD1 LEU B 132 30.910 17.098 19.066 1.00 37.86 B C ATOM 2508 CD2 LEU B 132 30.862 14.813 18.103 1.00 34.59 B C ATOM 2509 C LEU B 132 35.266 14.862 19.522 1.00 44.40 B C ATOM 2510 O LEU B 132 35.934 15.249 20.484 1.00 49.72 B O ATOM 2511 N PRO B 133 35.782 14.716 18.291 1.00 43.45 B N ATOM 2512 CD PRO B 133 35.117 14.075 17.144 1.00 43.13 B C ATOM 2513 CA PRO B 133 37.159 15.115 17.974 1.00 37.84 B C ATOM 2514 CB PRO B 133 37.319 14.693 16.514 1.00 35.64 B C ATOM 2515 CG PRO B 133 36.275 13.637 16.299 1.00 40.82 B C ATOM 2516 C PRO B 133 37.329 16.626 18.107 1.00 39.64 B C ATOM 2517 O PRO B 133 36.462 17.376 17.678 1.00 42.21 B O ATOM 2518 N ARG B 134 38.436 17.056 18.698 1.00 39.72 B N ATOM 2519 CA ARG B 134 38.669 18.463 18.984 1.00 39.48 B C ATOM 2520 CB ARG B 134 40.135 18.698 19.350 1.00 34.26 B C ATOM 2521 CG ARG B 134 40.466 18.294 20.763 1.00 45.79 B C ATOM 2522 CD ARG B 134 41.765 18.916 21.220 1.00 52.96 B C ATOM 2523 NE ARG B 134 42.005 18.669 22.637 1.00 60.26 B N ATOM 2524 CZ ARG B 134 42.898 19.329 23.366 1.00 61.56 B C ATOM 2525 NH1 ARG B 134 43.631 20.286 22.811 1.00 57.81 B N ATOM 2526 NH2 ARG B 134 43.051 19.038 24.652 1.00 60.79 B N ATOM 2527 C ARG B 134 38.263 19.390 17.847 1.00 46.22 B C ATOM 2528 O ARG B 134 37.752 20.491 18.091 1.00 45.48 B O ATOM 2529 N ALA B 135 38.497 18.946 16.613 1.00 41.61 B N ATOM 2530 CA ALA B 135 38.189 19.748 15.430 1.00 46.44 B C ATOM 2531 CB ALA B 135 39.111 19.375 14.259 1.00 40.60 B C ATOM 2532 C ALA B 135 36.714 19.681 15.011 1.00 44.61 B C ATOM 2533 O ALA B 135 36.253 20.497 14.213 1.00 47.22 B O ATOM 2534 N VAL B 136 35.969 18.721 15.538 1.00 43.97 B N ATOM 2535 CA VAL B 136 34.528 18.738 15.314 1.00 46.49 B C ATOM 2536 CB VAL B 136 33.879 17.356 15.519 1.00 41.37 B C ATOM 2537 CG1 VAL B 136 32.398 17.422 15.220 1.00 35.84 B C ATOM 2538 CG2 VAL B 136 34.534 16.345 14.604 1.00 41.58 B C ATOM 2539 C VAL B 136 33.924 19.796 16.228 1.00 42.03 B C ATOM 2540 O VAL B 136 32.978 20.491 15.862 1.00 42.92 B O ATOM 2541 N ILE B 137 34.514 19.933 17.408 1.00 45.12 B N ATOM 2542 CA ILE B 137 34.128 20.967 18.365 1.00 41.50 B C ATOM 2543 CB ILE B 137 34.788 20.721 19.739 1.00 42.58 B C ATOM 2544 CG2 ILE B 137 34.507 21.870 20.688 1.00 39.25 B C ATOM 2545 CG1 ILE B 137 34.308 19.383 20.326 1.00 41.50 B C ATOM 2546 CD1 ILE B 137 35.181 18.857 21.454 1.00 39.48 B C ATOM 2547 C ILE B 137 34.474 22.369 17.851 1.00 40.33 B C ATOM 2548 O ILE B 137 33.595 23.218 17.719 1.00 41.84 B O ATOM 2549 N ASP B 138 35.748 22.605 17.552 1.00 42.50 B N ATOM 2550 CA ASP B 138 36.177 23.873 16.960 1.00 40.93 B C ATOM 2551 CB ASP B 138 37.592 23.754 16.371 1.00 36.85 B C ATOM 2552 CG ASP B 138 38.625 23.281 17.383 1.00 44.46 B C ATOM 2553 OD1 ASP B 138 38.298 23.151 18.579 1.00 50.63 B O ATOM 2554 OD2 ASP B 138 39.780 23.033 16.977 1.00 55.49 B O ATOM 2555 C ASP B 138 35.214 24.310 15.853 1.00 38.85 B C ATOM 2556 O ASP B 138 34.782 25.466 15.789 1.00 38.98 B O ATOM 2557 N ASP B 139 34.877 23.364 14.988 1.00 39.23 B N ATOM 2558 CA ASP B 139 34.075 23.641 13.812 1.00 38.85 B C ATOM 2559 CB ASP B 139 34.174 22.465 12.843 1.00 35.18 B C ATOM 2560 CG ASP B 139 33.258 22.613 11.661 1.00 36.65 B C ATOM 2561 OD1 ASP B 139 33.619 23.345 10.716 1.00 42.68 B O ATOM 2562 OD2 ASP B 139 32.179 21.987 11.674 1.00 37.93 B O ATOM 2563 C ASP B 139 32.610 23.932 14.147 1.00 42.00 B C ATOM 2564 O ASP B 139 31.984 24.792 13.522 1.00 41.56 B O ATOM 2565 N ALA B 140 32.058 23.218 15.125 1.00 39.23 B N ATOM 2566 CA ALA B 140 30.673 23.454 15.519 1.00 40.19 B C ATOM 2567 CB ALA B 140 30.177 22.368 16.472 1.00 44.25 B C ATOM 2568 C ALA B 140 30.530 24.836 16.151 1.00 39.77 B C ATOM 2569 O ALA B 140 29.497 25.493 16.003 1.00 38.61 B O ATOM 2570 N PHE B 141 31.566 25.272 16.860 1.00 39.21 B N ATOM 2571 CA PHE B 141 31.575 26.620 17.416 1.00 44.29 B C ATOM 2572 CB PHE B 141 32.654 26.776 18.488 1.00 40.07 B C ATOM 2573 CG PHE B 141 32.406 25.967 19.716 1.00 44.25 B C ATOM 2574 CD1 PHE B 141 31.122 25.786 20.191 1.00 40.25 B C ATOM 2575 CD2 PHE B 141 33.466 25.394 20.412 1.00 46.22 B C ATOM 2576 CE1 PHE B 141 30.900 25.032 21.337 1.00 48.37 B C ATOM 2577 CE2 PHE B 141 33.252 24.646 21.556 1.00 39.72 B C ATOM 2578 CZ PHE B 141 31.972 24.463 22.022 1.00 43.12 B C ATOM 2579 C PHE B 141 31.770 27.671 16.320 1.00 42.30 B C ATOM 2580 O PHE B 141 31.129 28.728 16.341 1.00 42.04 B O ATOM 2581 N ALA B 142 32.658 27.391 15.371 1.00 36.56 B N ATOM 2582 CA ALA B 142 32.864 28.318 14.256 1.00 42.91 B C ATOM 2583 CB ALA B 142 33.945 27.804 13.306 1.00 33.42 B C ATOM 2584 C ALA B 142 31.555 28.558 13.510 1.00 33.68 B C ATOM 2585 O ALA B 142 31.208 29.691 13.194 1.00 32.88 B O ATOM 2586 N ARG B 143 30.819 27.479 13.266 1.00 37.33 B N ATOM 2587 CA ARG B 143 29.551 27.541 12.540 1.00 34.79 B C ATOM 2588 CB ARG B 143 29.092 26.131 12.175 1.00 28.59 B C ATOM 2589 CG ARG B 143 29.982 25.494 11.128 1.00 34.05 B C ATOM 2590 CD ARG B 143 30.004 23.982 11.206 1.00 36.62 B C ATOM 2591 NE ARG B 143 28.673 23.424 11.045 1.00 39.62 B N ATOM 2592 CZ ARG B 143 28.159 22.499 11.838 1.00 39.89 B C ATOM 2593 NH1 ARG B 143 28.879 22.000 12.838 1.00 40.33 B N ATOM 2594 NH2 ARG B 143 26.934 22.060 11.612 1.00 43.27 B N ATOM 2595 C ARG B 143 28.461 28.292 13.301 1.00 38.47 B C ATOM 2596 O ARG B 143 27.743 29.111 12.725 1.00 43.47 B O ATOM 2597 N ALA B 144 28.329 28.019 14.592 1.00 31.03 B N ATOM 2598 CA ALA B 144 27.395 28.780 15.397 1.00 32.58 B C ATOM 2599 CB ALA B 144 27.496 28.366 16.852 1.00 42.03 B C ATOM 2600 C ALA B 144 27.615 30.290 15.247 1.00 33.31 B C ATOM 2601 O ALA B 144 26.674 31.045 14.996 1.00 37.33 B O ATOM 2602 N PHE B 145 28.856 30.732 15.402 1.00 34.57 B N ATOM 2603 CA PHE B 145 29.169 32.151 15.277 1.00 35.40 B C ATOM 2604 CB PHE B 145 30.628 32.425 15.662 1.00 34.39 B C ATOM 2605 CG PHE B 145 30.881 32.367 17.141 1.00 36.43 B C ATOM 2606 CD1 PHE B 145 30.177 33.181 18.007 1.00 32.92 B C ATOM 2607 CD2 PHE B 145 31.828 31.502 17.667 1.00 40.02 B C ATOM 2608 CE1 PHE B 145 30.402 33.125 19.368 1.00 32.33 B C ATOM 2609 CE2 PHE B 145 32.057 31.443 19.030 1.00 34.61 B C ATOM 2610 CZ PHE B 145 31.346 32.260 19.878 1.00 36.72 B C ATOM 2611 C PHE B 145 28.863 32.693 13.877 1.00 33.93 B C ATOM 2612 O PHE B 145 28.481 33.852 13.720 1.00 36.70 B O ATOM 2613 N ALA B 146 29.021 31.852 12.864 1.00 31.41 B N ATOM 2614 CA ALA B 146 28.779 32.279 11.490 1.00 31.63 B C ATOM 2615 CB ALA B 146 29.433 31.332 10.518 1.00 25.44 B C ATOM 2616 C ALA B 146 27.294 32.434 11.163 1.00 38.07 B C ATOM 2617 O ALA B 146 26.952 32.987 10.107 1.00 43.68 B O ATOM 2618 N LEU B 147 26.417 31.934 12.040 1.00 29.99 B N ATOM 2619 CA LEU B 147 24.987 32.219 11.926 1.00 29.38 B C ATOM 2620 CB LEU B 147 24.152 31.338 12.855 1.00 31.83 B C ATOM 2621 CG LEU B 147 23.960 29.853 12.561 1.00 37.60 B C ATOM 2622 CD1 LEU B 147 23.435 29.167 13.800 1.00 27.62 B C ATOM 2623 CD2 LEU B 147 23.041 29.627 11.361 1.00 26.68 B C ATOM 2624 C LEU B 147 24.746 33.659 12.319 1.00 34.14 B C ATOM 2625 O LEU B 147 24.024 34.391 11.634 1.00 33.22 B O ATOM 2626 N TRP B 148 25.356 34.046 13.439 1.00 33.33 B N ATOM 2627 CA TRP B 148 25.103 35.331 14.068 1.00 34.62 B C ATOM 2628 CB TRP B 148 25.461 35.273 15.560 1.00 33.73 B C ATOM 2629 CG TRP B 148 24.536 34.370 16.358 1.00 42.62 B C ATOM 2630 CD2 TRP B 148 23.134 34.578 16.621 1.00 34.51 B C ATOM 2631 CE2 TRP B 148 22.685 33.484 17.382 1.00 31.47 B C ATOM 2632 CE3 TRP B 148 22.220 35.584 16.288 1.00 33.64 B C ATOM 2633 CD1 TRP B 148 24.862 33.186 16.963 1.00 33.85 B C ATOM 2634 NE1 TRP B 148 23.757 32.653 17.575 1.00 33.77 B N ATOM 2635 CZ2 TRP B 148 21.362 33.364 17.820 1.00 34.08 B C ATOM 2636 CZ3 TRP B 148 20.899 35.459 16.722 1.00 33.77 B C ATOM 2637 CH2 TRP B 148 20.488 34.358 17.476 1.00 26.80 B C ATOM 2638 C TRP B 148 25.863 36.457 13.385 1.00 34.38 B C ATOM 2639 O TRP B 148 25.477 37.618 13.455 1.00 34.89 B O ATOM 2640 N SER B 149 26.952 36.106 12.725 1.00 34.89 B N ATOM 2641 CA SER B 149 27.780 37.102 12.063 1.00 37.77 B C ATOM 2642 CB SER B 149 29.110 36.477 11.654 1.00 32.84 B C ATOM 2643 OG SER B 149 29.711 37.242 10.634 1.00 44.99 B O ATOM 2644 C SER B 149 27.088 37.715 10.844 1.00 36.20 B C ATOM 2645 O SER B 149 27.028 38.932 10.699 1.00 41.48 B O ATOM 2646 N ALA B 150 26.567 36.865 9.971 1.00 33.94 B N ATOM 2647 CA ALA B 150 25.904 37.318 8.753 1.00 33.34 B C ATOM 2648 CB ALA B 150 25.418 36.120 7.963 1.00 29.49 B C ATOM 2649 C ALA B 150 24.734 38.261 9.019 1.00 35.61 B C ATOM 2650 O ALA B 150 24.268 38.949 8.107 1.00 32.62 B O ATOM 2651 N VAL B 151 24.243 38.269 10.258 1.00 33.12 B N ATOM 2652 CA VAL B 151 22.993 38.954 10.586 1.00 32.35 B C ATOM 2653 CB VAL B 151 21.948 37.993 11.202 1.00 35.06 B C ATOM 2654 CG1 VAL B 151 21.318 37.118 10.129 1.00 25.89 B C ATOM 2655 CG2 VAL B 151 22.578 37.160 12.318 1.00 31.20 B C ATOM 2656 C VAL B 151 23.200 40.115 11.543 1.00 31.88 B C ATOM 2657 O VAL B 151 22.243 40.797 11.898 1.00 32.20 B O ATOM 2658 N THR B 152 24.452 40.324 11.946 1.00 34.50 B N ATOM 2659 CA THR B 152 24.830 41.412 12.841 1.00 33.93 B C ATOM 2660 CB THR B 152 25.161 40.901 14.263 1.00 34.13 B C ATOM 2661 OG1 THR B 152 26.472 40.322 14.283 1.00 31.86 B O ATOM 2662 CG2 THR B 152 24.151 39.887 14.708 1.00 31.66 B C ATOM 2663 C THR B 152 26.060 42.135 12.309 1.00 35.18 B C ATOM 2664 O THR B 152 26.693 41.670 11.360 1.00 37.27 B O ATOM 2665 N PRO B 153 26.396 43.285 12.914 1.00 33.61 B N ATOM 2666 CD PRO B 153 25.540 44.083 13.804 1.00 35.29 B C ATOM 2667 CA PRO B 153 27.641 43.986 12.603 1.00 35.48 B C ATOM 2668 CB PRO B 153 27.373 45.418 13.099 1.00 33.59 B C ATOM 2669 CG PRO B 153 25.922 45.469 13.447 1.00 40.01 B C ATOM 2670 C PRO B 153 28.817 43.391 13.380 1.00 37.59 B C ATOM 2671 O PRO B 153 29.749 44.108 13.737 1.00 38.95 B O ATOM 2672 N LEU B 154 28.785 42.092 13.645 1.00 35.39 B N ATOM 2673 CA LEU B 154 29.873 41.494 14.403 1.00 37.49 B C ATOM 2674 CB LEU B 154 29.348 40.905 15.713 1.00 40.60 B C ATOM 2675 CG LEU B 154 28.620 41.899 16.616 1.00 37.22 B C ATOM 2676 CD1 LEU B 154 28.184 41.225 17.904 1.00 40.85 B C ATOM 2677 CD2 LEU B 154 29.497 43.094 16.914 1.00 34.40 B C ATOM 2678 C LEU B 154 30.698 40.456 13.635 1.00 42.35 B C ATOM 2679 O LEU B 154 30.176 39.727 12.782 1.00 40.30 B O ATOM 2680 N THR B 155 31.997 40.431 13.933 1.00 36.06 B N ATOM 2681 CA THR B 155 32.882 39.350 13.527 1.00 38.75 B C ATOM 2682 CB THR B 155 34.113 39.856 12.722 1.00 40.50 B C ATOM 2683 OG1 THR B 155 34.902 40.723 13.543 1.00 49.90 B O ATOM 2684 CG2 THR B 155 33.696 40.595 11.467 1.00 28.86 B C ATOM 2685 C THR B 155 33.381 38.640 14.782 1.00 37.09 B C ATOM 2686 O THR B 155 33.595 39.269 15.813 1.00 45.28 B O ATOM 2687 N PHE B 156 33.581 37.333 14.689 1.00 39.72 B N ATOM 2688 CA PHE B 156 34.015 36.538 15.835 1.00 41.10 B C ATOM 2689 CB PHE B 156 32.945 35.501 16.207 1.00 35.76 B C ATOM 2690 CG PHE B 156 31.583 36.097 16.472 1.00 38.58 B C ATOM 2691 CD1 PHE B 156 30.663 36.246 15.440 1.00 35.22 B C ATOM 2692 CD2 PHE B 156 31.229 36.514 17.748 1.00 33.15 B C ATOM 2693 CE1 PHE B 156 29.424 36.796 15.670 1.00 32.35 B C ATOM 2694 CE2 PHE B 156 29.985 37.069 17.991 1.00 34.02 B C ATOM 2695 CZ PHE B 156 29.080 37.209 16.949 1.00 36.26 B C ATOM 2696 C PHE B 156 35.350 35.843 15.569 1.00 40.45 B C ATOM 2697 O PHE B 156 35.433 34.959 14.730 1.00 40.21 B O ATOM 2698 N THR B 157 36.386 36.249 16.295 1.00 37.91 B N ATOM 2699 CA THR B 157 37.703 35.641 16.172 1.00 40.14 B C ATOM 2700 CB THR B 157 38.814 36.696 16.226 1.00 45.87 B C ATOM 2701 OG1 THR B 157 38.708 37.574 15.102 1.00 53.48 B O ATOM 2702 CG2 THR B 157 40.178 36.015 16.219 1.00 40.61 B C ATOM 2703 C THR B 157 37.985 34.690 17.319 1.00 45.36 B C ATOM 2704 O THR B 157 37.757 35.030 18.479 1.00 44.14 B O ATOM 2705 N ARG B 158 38.502 33.508 17.000 1.00 46.85 B N ATOM 2706 CA ARG B 158 38.929 32.572 18.033 1.00 42.93 B C ATOM 2707 CB ARG B 158 38.921 31.141 17.501 1.00 42.43 B C ATOM 2708 CG ARG B 158 39.632 30.170 18.424 1.00 43.77 B C ATOM 2709 CD ARG B 158 39.762 28.783 17.828 1.00 42.00 B C ATOM 2710 NE ARG B 158 40.458 27.899 18.757 1.00 43.13 B N ATOM 2711 CZ ARG B 158 40.652 26.601 18.554 1.00 45.87 B C ATOM 2712 NH1 ARG B 158 40.196 26.030 17.450 1.00 40.20 B N ATOM 2713 NH2 ARG B 158 41.292 25.871 19.462 1.00 48.03 B N ATOM 2714 C ARG B 158 40.335 32.908 18.510 1.00 44.60 B C ATOM 2715 O ARG B 158 41.255 33.010 17.704 1.00 46.17 B O ATOM 2716 N VAL B 159 40.505 33.076 19.816 1.00 41.59 B N ATOM 2717 CA VAL B 159 41.836 33.289 20.374 1.00 43.66 B C ATOM 2718 CB VAL B 159 41.918 34.632 21.100 1.00 41.73 B C ATOM 2719 CG1 VAL B 159 41.350 35.737 20.214 1.00 40.38 B C ATOM 2720 CG2 VAL B 159 41.168 34.560 22.416 1.00 45.42 B C ATOM 2721 C VAL B 159 42.250 32.155 21.324 1.00 44.45 B C ATOM 2722 O VAL B 159 41.452 31.275 21.643 1.00 42.73 B O ATOM 2723 N TYR B 160 43.501 32.176 21.771 1.00 43.06 B N ATOM 2724 CA TYR B 160 44.011 31.130 22.656 1.00 40.60 B C ATOM 2725 CB TYR B 160 45.095 30.323 21.943 1.00 42.08 B C ATOM 2726 CG TYR B 160 44.574 29.680 20.675 1.00 39.79 B C ATOM 2727 CD1 TYR B 160 44.348 30.436 19.537 1.00 38.54 B C ATOM 2728 CE1 TYR B 160 43.855 29.865 18.385 1.00 38.44 B C ATOM 2729 CD2 TYR B 160 44.273 28.333 20.629 1.00 36.72 B C ATOM 2730 CE2 TYR B 160 43.782 27.756 19.479 1.00 40.75 B C ATOM 2731 CZ TYR B 160 43.574 28.527 18.361 1.00 36.20 B C ATOM 2732 OH TYR B 160 43.088 27.956 17.211 1.00 37.41 B O ATOM 2733 C TYR B 160 44.502 31.704 23.988 1.00 44.59 B C ATOM 2734 O TYR B 160 45.160 31.028 24.777 1.00 46.58 B O ATOM 2735 N SER B 161 44.154 32.960 24.229 1.00 43.48 B N ATOM 2736 CA SER B 161 44.433 33.619 25.493 1.00 48.74 B C ATOM 2737 CB SER B 161 44.916 35.035 25.220 1.00 50.11 B C ATOM 2738 OG SER B 161 44.009 35.701 24.355 1.00 48.11 B O ATOM 2739 C SER B 161 43.148 33.680 26.314 1.00 51.38 B C ATOM 2740 O SER B 161 42.057 33.608 25.761 1.00 54.19 B O ATOM 2741 N ARG B 162 43.273 33.807 27.631 1.00 57.09 B N ATOM 2742 CA ARG B 162 42.109 34.045 28.483 1.00 54.46 B C ATOM 2743 CB ARG B 162 42.402 33.683 29.938 1.00 50.75 B C ATOM 2744 CG ARG B 162 43.570 34.421 30.557 1.00 54.15 B C ATOM 2745 CD ARG B 162 43.171 35.803 31.021 1.00 54.39 B C ATOM 2746 NE ARG B 162 44.338 36.662 31.160 1.00 68.06 B N ATOM 2747 CZ ARG B 162 44.284 37.958 31.437 1.00 62.11 B C ATOM 2748 NH1 ARG B 162 43.111 38.547 31.613 1.00 61.20 B N ATOM 2749 NH2 ARG B 162 45.405 38.661 31.538 1.00 65.78 B N ATOM 2750 C ARG B 162 41.683 35.501 28.349 1.00 58.39 B C ATOM 2751 O ARG B 162 40.726 35.948 28.980 1.00 53.60 B O ATOM 2752 N ASP B 163 42.423 36.231 27.520 1.00 62.85 B N ATOM 2753 CA ASP B 163 42.030 37.560 27.079 1.00 66.16 B C ATOM 2754 CB ASP B 163 43.248 38.318 26.524 1.00 65.73 B C ATOM 2755 CG ASP B 163 42.901 39.724 26.030 1.00 80.17 B C ATOM 2756 OD1 ASP B 163 41.744 40.162 26.220 1.00 79.18 B O ATOM 2757 OD2 ASP B 163 43.789 40.392 25.452 1.00 76.77 B O ATOM 2758 C ASP B 163 40.967 37.389 25.996 1.00 63.62 B C ATOM 2759 O ASP B 163 41.266 37.482 24.796 1.00 59.65 B O ATOM 2760 N ALA B 164 39.734 37.117 26.422 1.00 51.47 B N ATOM 2761 CA ALA B 164 38.631 36.915 25.483 1.00 49.69 B C ATOM 2762 CB ALA B 164 38.626 35.483 24.956 1.00 47.46 B C ATOM 2763 C ALA B 164 37.265 37.271 26.066 1.00 51.22 B C ATOM 2764 O ALA B 164 37.022 37.107 27.263 1.00 49.18 B O ATOM 2765 N ASP B 165 36.380 37.752 25.197 1.00 49.35 B N ATOM 2766 CA ASP B 165 35.020 38.121 25.569 1.00 44.53 B C ATOM 2767 CB ASP B 165 34.349 38.851 24.399 1.00 40.89 B C ATOM 2768 CG ASP B 165 35.162 40.035 23.899 1.00 48.66 B C ATOM 2769 OD1 ASP B 165 35.631 40.834 24.738 1.00 54.11 B O ATOM 2770 OD2 ASP B 165 35.321 40.178 22.663 1.00 43.94 B O ATOM 2771 C ASP B 165 34.187 36.891 25.947 1.00 44.06 B C ATOM 2772 O ASP B 165 33.503 36.865 26.976 1.00 42.52 B O ATOM 2773 N ILE B 166 34.242 35.879 25.092 1.00 38.70 B N ATOM 2774 CA ILE B 166 33.434 34.681 25.248 1.00 40.09 B C ATOM 2775 CB ILE B 166 32.635 34.402 23.957 1.00 39.77 B C ATOM 2776 CG2 ILE B 166 32.076 32.962 23.932 1.00 32.15 B C ATOM 2777 CG1 ILE B 166 31.543 35.459 23.785 1.00 40.62 B C ATOM 2778 CD1 ILE B 166 30.969 35.531 22.382 1.00 43.36 B C ATOM 2779 C ILE B 166 34.316 33.481 25.564 1.00 43.67 B C ATOM 2780 O ILE B 166 34.941 32.912 24.669 1.00 44.03 B O ATOM 2781 N VAL B 167 34.385 33.099 26.835 1.00 40.56 B N ATOM 2782 CA VAL B 167 35.142 31.907 27.183 1.00 43.55 B C ATOM 2783 CB VAL B 167 35.820 32.020 28.548 1.00 44.36 B C ATOM 2784 CG1 VAL B 167 36.403 30.673 28.945 1.00 43.21 B C ATOM 2785 CG2 VAL B 167 36.905 33.079 28.501 1.00 42.28 B C ATOM 2786 C VAL B 167 34.244 30.688 27.162 1.00 40.78 B C ATOM 2787 O VAL B 167 33.297 30.603 27.939 1.00 45.31 B O ATOM 2788 N ILE B 168 34.536 29.751 26.263 1.00 39.57 B N ATOM 2789 CA ILE B 168 33.772 28.512 26.172 1.00 39.97 B C ATOM 2790 CB ILE B 168 33.828 27.938 24.772 1.00 42.34 B C ATOM 2791 CG2 ILE B 168 33.161 26.568 24.732 1.00 44.20 B C ATOM 2792 CG1 ILE B 168 33.180 28.893 23.776 1.00 45.33 B C ATOM 2793 CD1 ILE B 168 33.616 28.621 22.344 1.00 43.76 B C ATOM 2794 C ILE B 168 34.316 27.457 27.130 1.00 44.53 B C ATOM 2795 O ILE B 168 35.528 27.336 27.299 1.00 46.20 B O ATOM 2796 N GLN B 169 33.422 26.693 27.751 1.00 43.06 B N ATOM 2797 CA GLN B 169 33.827 25.700 28.740 1.00 44.66 B C ATOM 2798 CB GLN B 169 33.982 26.348 30.116 1.00 43.34 B C ATOM 2799 CG GLN B 169 34.202 25.340 31.236 1.00 47.07 B C ATOM 2800 CD GLN B 169 34.097 25.955 32.625 1.00 51.75 B C ATOM 2801 OE1 GLN B 169 33.675 27.100 32.782 1.00 51.62 B O ATOM 2802 NE2 GLN B 169 34.479 25.189 33.642 1.00 51.96 B N ATOM 2803 C GLN B 169 32.884 24.503 28.859 1.00 46.19 B C ATOM 2804 O GLN B 169 31.665 24.656 28.931 1.00 48.58 B O ATOM 2805 N PHE B 170 33.467 23.311 28.897 1.00 45.67 B N ATOM 2806 CA PHE B 170 32.735 22.102 29.235 1.00 40.96 B C ATOM 2807 CB PHE B 170 33.238 20.931 28.392 1.00 46.03 B C ATOM 2808 CG PHE B 170 32.888 21.030 26.934 1.00 43.00 B C ATOM 2809 CD1 PHE B 170 33.678 21.768 26.066 1.00 45.97 B C ATOM 2810 CD2 PHE B 170 31.775 20.379 26.430 1.00 42.44 B C ATOM 2811 CE1 PHE B 170 33.368 21.857 24.716 1.00 41.65 B C ATOM 2812 CE2 PHE B 170 31.452 20.467 25.083 1.00 39.21 B C ATOM 2813 CZ PHE B 170 32.256 21.205 24.226 1.00 42.19 B C ATOM 2814 C PHE B 170 32.949 21.796 30.711 1.00 43.48 B C ATOM 2815 O PHE B 170 34.080 21.838 31.196 1.00 42.06 B O ATOM 2816 N GLY B 171 31.868 21.488 31.425 1.00 44.89 B N ATOM 2817 CA GLY B 171 31.963 21.199 32.846 1.00 42.34 B C ATOM 2818 C GLY B 171 30.835 20.321 33.350 1.00 48.05 B C ATOM 2819 O GLY B 171 29.768 20.264 32.745 1.00 52.63 B O ATOM 2820 N VAL B 172 31.066 19.629 34.459 1.00 47.23 B N ATOM 2821 CA VAL B 172 30.035 18.765 35.036 1.00 50.19 B C ATOM 2822 CB VAL B 172 30.491 17.289 35.090 1.00 48.13 B C ATOM 2823 CG1 VAL B 172 30.175 16.581 33.783 1.00 46.92 B C ATOM 2824 CG2 VAL B 172 31.969 17.207 35.395 1.00 45.77 B C ATOM 2825 C VAL B 172 29.615 19.221 36.432 1.00 50.74 B C ATOM 2826 O VAL B 172 30.453 19.636 37.246 1.00 52.67 B O ATOM 2827 N ALA B 173 28.319 19.151 36.712 1.00 44.07 B N ATOM 2828 CA ALA B 173 27.835 19.540 38.028 1.00 49.14 B C ATOM 2829 CB ALA B 173 28.348 18.571 39.074 1.00 46.26 B C ATOM 2830 C ALA B 173 28.310 20.950 38.350 1.00 55.73 B C ATOM 2831 O ALA B 173 28.293 21.832 37.488 1.00 55.80 B O ATOM 2832 N GLU B 174 28.735 21.160 39.593 1.00 57.47 B N ATOM 2833 CA GLU B 174 29.381 22.410 39.976 1.00 55.99 B C ATOM 2834 CB GLU B 174 29.635 22.450 41.483 1.00 51.82 B C ATOM 2835 CG GLU B 174 30.499 23.608 41.929 1.00 54.91 B C ATOM 2836 CD GLU B 174 29.758 24.935 41.935 1.00 61.90 B C ATOM 2837 OE1 GLU B 174 28.645 24.998 42.509 1.00 57.17 B O ATOM 2838 OE2 GLU B 174 30.302 25.919 41.378 1.00 58.73 B O ATOM 2839 C GLU B 174 30.693 22.512 39.206 1.00 57.40 B C ATOM 2840 O GLU B 174 31.535 21.611 39.267 1.00 54.64 B O ATOM 2841 N HIS B 175 30.857 23.597 38.460 1.00 57.49 B N ATOM 2842 CA HIS B 175 31.982 23.705 37.543 1.00 44.72 B C ATOM 2843 CB HIS B 175 31.530 23.453 36.098 1.00 42.64 B C ATOM 2844 CG HIS B 175 30.330 24.252 35.685 1.00 45.53 B C ATOM 2845 CD2 HIS B 175 30.214 25.342 34.891 1.00 41.79 B C ATOM 2846 ND1 HIS B 175 29.051 23.945 36.099 1.00 48.06 B N ATOM 2847 CE1 HIS B 175 28.201 24.812 35.580 1.00 41.78 B C ATOM 2848 NE2 HIS B 175 28.880 25.671 34.845 1.00 39.88 B N ATOM 2849 C HIS B 175 32.689 25.043 37.677 1.00 48.27 B C ATOM 2850 O HIS B 175 33.553 25.380 36.867 1.00 50.09 B O ATOM 2851 N GLY B 176 32.321 25.808 38.702 1.00 52.16 B N ATOM 2852 CA GLY B 176 33.081 26.993 39.063 1.00 43.07 B C ATOM 2853 C GLY B 176 32.326 28.303 39.129 1.00 46.08 B C ATOM 2854 O GLY B 176 32.943 29.363 39.061 1.00 40.72 B O ATOM 2855 N ASP B 177 31.003 28.248 39.275 1.00 48.62 B N ATOM 2856 CA ASP B 177 30.197 29.472 39.279 1.00 44.01 B C ATOM 2857 CB ASP B 177 29.889 29.933 37.848 1.00 41.94 B C ATOM 2858 CG ASP B 177 29.104 28.905 37.050 1.00 47.06 B C ATOM 2859 OD1 ASP B 177 28.866 27.787 37.558 1.00 44.94 B O ATOM 2860 OD2 ASP B 177 28.727 29.219 35.901 1.00 47.72 B O ATOM 2861 C ASP B 177 28.907 29.359 40.087 1.00 51.23 B C ATOM 2862 O ASP B 177 28.091 30.280 40.107 1.00 50.83 B O ATOM 2863 N GLY B 178 28.721 28.230 40.755 1.00 51.61 B N ATOM 2864 CA GLY B 178 27.546 28.053 41.581 1.00 52.55 B C ATOM 2865 C GLY B 178 26.259 28.141 40.786 1.00 58.22 B C ATOM 2866 O GLY B 178 25.198 28.471 41.326 1.00 60.58 B O ATOM 2867 N TYR B 179 26.359 27.864 39.492 1.00 51.97 B N ATOM 2868 CA TYR B 179 25.193 27.567 38.680 1.00 46.35 B C ATOM 2869 CB TYR B 179 25.042 28.566 37.543 1.00 41.86 B C ATOM 2870 CG TYR B 179 24.706 29.972 37.965 1.00 43.83 B C ATOM 2871 CD1 TYR B 179 25.652 30.976 37.876 1.00 44.97 B C ATOM 2872 CE1 TYR B 179 25.361 32.270 38.239 1.00 44.18 B C ATOM 2873 CD2 TYR B 179 23.438 30.305 38.426 1.00 46.17 B C ATOM 2874 CE2 TYR B 179 23.134 31.612 38.795 1.00 46.68 B C ATOM 2875 CZ TYR B 179 24.109 32.591 38.697 1.00 44.80 B C ATOM 2876 OH TYR B 179 23.860 33.899 39.062 1.00 41.72 B O ATOM 2877 C TYR B 179 25.426 26.184 38.099 1.00 49.16 B C ATOM 2878 O TYR B 179 25.513 26.026 36.885 1.00 50.26 B O ATOM 2879 N PRO B 180 25.533 25.176 38.975 1.00 52.31 B N ATOM 2880 CD PRO B 180 25.049 25.254 40.364 1.00 54.19 B C ATOM 2881 CA PRO B 180 25.972 23.822 38.619 1.00 46.42 B C ATOM 2882 CB PRO B 180 25.927 23.072 39.961 1.00 55.60 B C ATOM 2883 CG PRO B 180 25.738 24.115 41.022 1.00 55.32 B C ATOM 2884 C PRO B 180 25.016 23.153 37.644 1.00 48.18 B C ATOM 2885 O PRO B 180 23.836 23.502 37.630 1.00 53.31 B O ATOM 2886 N PHE B 181 25.509 22.200 36.855 1.00 50.24 B N ATOM 2887 CA PHE B 181 24.640 21.419 35.972 1.00 48.65 B C ATOM 2888 C PHE B 181 24.031 20.227 36.712 1.00 50.88 B C ATOM 2889 CB PHE B 181 25.393 20.929 34.738 1.00 47.06 B C ATOM 2890 CG PHE B 181 25.921 22.030 33.870 1.00 47.77 B C ATOM 2891 CD1 PHE B 181 25.091 23.053 33.442 1.00 48.13 B C ATOM 2892 CD2 PHE B 181 27.251 22.033 33.466 1.00 48.92 B C ATOM 2893 CE1 PHE B 181 25.578 24.070 32.638 1.00 42.30 B C ATOM 2894 CE2 PHE B 181 27.749 23.047 32.661 1.00 42.34 B C ATOM 2895 CZ PHE B 181 26.909 24.068 32.248 1.00 46.60 B C ATOM 2896 O PHE B 181 24.172 20.102 37.928 1.00 48.68 B O ATOM 2897 N ASP B 182 23.370 19.345 35.968 1.00 52.28 B N ATOM 2898 CA ASP B 182 22.610 18.248 36.567 1.00 49.03 B C ATOM 2899 CB ASP B 182 21.123 18.611 36.604 1.00 53.03 B C ATOM 2900 CG ASP B 182 20.594 19.051 35.243 1.00 48.84 B C ATOM 2901 OD1 ASP B 182 21.001 20.125 34.769 1.00 51.57 B O ATOM 2902 OD2 ASP B 182 19.767 18.334 34.645 1.00 49.97 B O ATOM 2903 C ASP B 182 22.770 16.944 35.797 1.00 48.62 B C ATOM 2904 O ASP B 182 21.840 16.498 35.133 1.00 56.89 B O ATOM 2905 N GLY B 183 23.944 16.334 35.876 1.00 48.83 B N ATOM 2906 CA GLY B 183 24.173 15.066 35.206 1.00 51.53 B C ATOM 2907 C GLY B 183 23.447 14.934 33.878 1.00 50.37 B C ATOM 2908 O GLY B 183 23.465 15.846 33.065 1.00 47.97 B O ATOM 2909 N LYS B 184 22.796 13.798 33.656 1.00 54.02 B N ATOM 2910 CA LYS B 184 22.202 13.527 32.351 1.00 54.69 B C ATOM 2911 CB LYS B 184 22.062 12.020 32.103 1.00 50.22 B C ATOM 2912 CG LYS B 184 21.265 11.700 30.846 1.00 55.82 B C ATOM 2913 CD LYS B 184 21.489 10.279 30.355 1.00 62.30 B C ATOM 2914 CE LYS B 184 20.546 9.292 31.014 1.00 54.49 B C ATOM 2915 NZ LYS B 184 20.863 7.904 30.565 1.00 49.38 B N ATOM 2916 C LYS B 184 20.864 14.228 32.133 1.00 50.03 B C ATOM 2917 O LYS B 184 20.000 14.213 33.001 1.00 47.67 B O ATOM 2918 N ASP B 185 20.714 14.838 30.960 1.00 52.04 B N ATOM 2919 CA ASP B 185 19.471 15.501 30.562 1.00 49.55 B C ATOM 2920 CB ASP B 185 18.334 14.486 30.491 1.00 47.32 B C ATOM 2921 CG ASP B 185 18.639 13.351 29.539 1.00 55.03 B C ATOM 2922 OD1 ASP B 185 19.783 13.301 29.034 1.00 52.08 B O ATOM 2923 OD2 ASP B 185 17.741 12.514 29.292 1.00 53.51 B O ATOM 2924 C ASP B 185 19.098 16.660 31.475 1.00 45.20 B C ATOM 2925 O ASP B 185 19.775 16.927 32.456 1.00 51.87 B O ATOM 2926 N GLY B 186 18.014 17.350 31.148 1.00 47.60 B N ATOM 2927 CA GLY B 186 17.554 18.456 31.967 1.00 49.59 B C ATOM 2928 C GLY B 186 18.143 19.765 31.485 1.00 49.74 B C ATOM 2929 O GLY B 186 17.844 20.212 30.380 1.00 44.77 B O ATOM 2930 N LEU B 187 18.971 20.384 32.320 1.00 50.57 B N ATOM 2931 CA LEU B 187 19.734 21.547 31.898 1.00 49.94 B C ATOM 2932 CB LEU B 187 20.384 22.243 33.092 1.00 49.22 B C ATOM 2933 CG LEU B 187 19.580 23.251 33.897 1.00 53.67 B C ATOM 2934 CD1 LEU B 187 18.299 22.608 34.396 1.00 55.66 B C ATOM 2935 CD2 LEU B 187 20.423 23.771 35.052 1.00 47.79 B C ATOM 2936 C LEU B 187 20.832 21.101 30.941 1.00 52.02 B C ATOM 2937 O LEU B 187 21.762 20.405 31.341 1.00 49.29 B O ATOM 2938 N LEU B 188 20.732 21.509 29.682 1.00 47.59 B N ATOM 2939 CA LEU B 188 21.762 21.195 28.710 1.00 40.48 B C ATOM 2940 CB LEU B 188 21.182 21.242 27.299 1.00 45.07 B C ATOM 2941 CG LEU B 188 20.157 20.123 27.125 1.00 50.89 B C ATOM 2942 CD1 LEU B 188 19.686 19.995 25.680 1.00 41.31 B C ATOM 2943 CD2 LEU B 188 20.755 18.809 27.636 1.00 45.67 B C ATOM 2944 C LEU B 188 22.980 22.110 28.844 1.00 41.35 B C ATOM 2945 O LEU B 188 24.117 21.635 28.890 1.00 44.85 B O ATOM 2946 N ALA B 189 22.744 23.415 28.918 1.00 33.97 B N ATOM 2947 CA ALA B 189 23.827 24.377 29.028 1.00 33.93 B C ATOM 2948 CB ALA B 189 24.556 24.492 27.699 1.00 43.52 B C ATOM 2949 C ALA B 189 23.292 25.732 29.445 1.00 35.04 B C ATOM 2950 O ALA B 189 22.086 25.911 29.566 1.00 41.17 B O ATOM 2951 N HIS B 190 24.187 26.689 29.662 1.00 36.65 B N ATOM 2952 CA HIS B 190 23.786 28.061 29.947 1.00 34.63 B C ATOM 2953 CB HIS B 190 23.386 28.231 31.422 1.00 46.41 B C ATOM 2954 CG HIS B 190 24.481 27.920 32.398 1.00 44.75 B C ATOM 2955 CD2 HIS B 190 25.548 28.648 32.803 1.00 46.86 B C ATOM 2956 ND1 HIS B 190 24.542 26.735 33.097 1.00 45.91 B N ATOM 2957 CE1 HIS B 190 25.599 26.745 33.887 1.00 43.00 B C ATOM 2958 NE2 HIS B 190 26.227 27.893 33.726 1.00 41.21 B N ATOM 2959 C HIS B 190 24.876 29.046 29.581 1.00 34.46 B C ATOM 2960 O HIS B 190 26.022 28.667 29.406 1.00 42.07 B O ATOM 2961 N ALA B 191 24.515 30.314 29.452 1.00 41.51 B N ATOM 2962 CA ALA B 191 25.484 31.349 29.090 1.00 43.48 B C ATOM 2963 CB ALA B 191 25.475 31.612 27.574 1.00 31.30 B C ATOM 2964 C ALA B 191 25.157 32.622 29.852 1.00 42.76 B C ATOM 2965 O ALA B 191 24.109 32.722 30.472 1.00 39.63 B O ATOM 2966 N PHE B 192 26.056 33.594 29.784 1.00 43.65 B N ATOM 2967 CA PHE B 192 25.905 34.838 30.517 1.00 41.11 B C ATOM 2968 CB PHE B 192 26.983 34.891 31.590 1.00 43.47 B C ATOM 2969 CG PHE B 192 27.070 33.625 32.406 1.00 44.44 B C ATOM 2970 CD1 PHE B 192 26.457 33.536 33.647 1.00 50.44 B C ATOM 2971 CD2 PHE B 192 27.736 32.518 31.921 1.00 42.77 B C ATOM 2972 CE1 PHE B 192 26.521 32.366 34.393 1.00 49.07 B C ATOM 2973 CE2 PHE B 192 27.803 31.351 32.659 1.00 46.30 B C ATOM 2974 CZ PHE B 192 27.195 31.275 33.898 1.00 49.02 B C ATOM 2975 C PHE B 192 25.984 36.036 29.565 1.00 42.69 B C ATOM 2976 O PHE B 192 26.758 36.018 28.612 1.00 41.40 B O ATOM 2977 N PRO B 193 25.174 37.081 29.812 1.00 45.64 B N ATOM 2978 CD PRO B 193 24.496 37.379 31.077 1.00 41.52 B C ATOM 2979 CA PRO B 193 25.053 38.197 28.862 1.00 45.70 B C ATOM 2980 CB PRO B 193 24.089 39.160 29.564 1.00 41.73 B C ATOM 2981 CG PRO B 193 23.505 38.399 30.664 1.00 48.56 B C ATOM 2982 C PRO B 193 26.392 38.893 28.612 1.00 41.65 B C ATOM 2983 O PRO B 193 27.357 38.667 29.348 1.00 41.71 B O ATOM 2984 N PRO B 194 26.457 39.729 27.572 1.00 40.24 B N ATOM 2985 CD PRO B 194 25.415 40.011 26.571 1.00 44.69 B C ATOM 2986 CA PRO B 194 27.711 40.422 27.267 1.00 44.34 B C ATOM 2987 CB PRO B 194 27.315 41.380 26.135 1.00 39.44 B C ATOM 2988 CG PRO B 194 26.181 40.719 25.468 1.00 41.39 B C ATOM 2989 C PRO B 194 28.232 41.204 28.468 1.00 39.87 B C ATOM 2990 O PRO B 194 27.455 41.694 29.271 1.00 37.37 B O ATOM 2991 N GLY B 195 29.547 41.315 28.582 1.00 47.17 B N ATOM 2992 CA GLY B 195 30.145 42.106 29.639 1.00 48.71 B C ATOM 2993 C GLY B 195 31.487 41.570 30.087 1.00 41.36 B C ATOM 2994 O GLY B 195 32.113 40.783 29.379 1.00 40.69 B O ATOM 2995 N PRO B 196 31.931 41.996 31.277 1.00 43.40 B N ATOM 2996 CD PRO B 196 31.238 43.035 32.048 1.00 49.89 B C ATOM 2997 CA PRO B 196 33.208 41.639 31.899 1.00 41.10 B C ATOM 2998 CB PRO B 196 33.470 42.811 32.857 1.00 43.13 B C ATOM 2999 CG PRO B 196 32.383 43.818 32.589 1.00 51.92 B C ATOM 3000 C PRO B 196 33.119 40.362 32.719 1.00 43.41 B C ATOM 3001 O PRO B 196 32.030 39.894 33.056 1.00 42.33 B O ATOM 3002 N GLY B 197 34.279 39.815 33.049 1.00 44.29 B N ATOM 3003 CA GLY B 197 34.362 38.650 33.900 1.00 41.34 B C ATOM 3004 C GLY B 197 33.814 37.411 33.240 1.00 42.48 B C ATOM 3005 O GLY B 197 34.206 37.055 32.131 1.00 40.92 B O ATOM 3006 N ILE B 198 32.911 36.743 33.944 1.00 45.32 B N ATOM 3007 CA ILE B 198 32.280 35.538 33.438 1.00 44.02 B C ATOM 3008 CB ILE B 198 31.574 34.769 34.576 1.00 47.53 B C ATOM 3009 CG2 ILE B 198 30.283 35.483 34.997 1.00 42.88 B C ATOM 3010 CG1 ILE B 198 31.299 33.321 34.160 1.00 51.07 B C ATOM 3011 CD1 ILE B 198 30.501 32.524 35.192 1.00 50.33 B C ATOM 3012 C ILE B 198 31.266 35.921 32.362 1.00 43.76 B C ATOM 3013 O ILE B 198 30.766 35.073 31.625 1.00 43.31 B O ATOM 3014 N GLN B 199 30.975 37.212 32.273 1.00 40.37 B N ATOM 3015 CA GLN B 199 29.950 37.686 31.361 1.00 44.09 B C ATOM 3016 CB GLN B 199 29.579 39.138 31.666 1.00 47.38 B C ATOM 3017 CG GLN B 199 28.424 39.278 32.645 1.00 39.09 B C ATOM 3018 CD GLN B 199 28.287 40.691 33.171 1.00 50.69 B C ATOM 3019 OE1 GLN B 199 27.473 41.476 32.677 1.00 44.79 B O ATOM 3020 NE2 GLN B 199 29.093 41.029 34.175 1.00 51.75 B N ATOM 3021 C GLN B 199 30.332 37.513 29.901 1.00 38.27 B C ATOM 3022 O GLN B 199 31.349 38.020 29.454 1.00 43.57 B O ATOM 3023 N GLY B 200 29.491 36.782 29.177 1.00 41.59 B N ATOM 3024 CA GLY B 200 29.689 36.502 27.771 1.00 38.06 B C ATOM 3025 C GLY B 200 30.083 35.057 27.534 1.00 40.77 B C ATOM 3026 O GLY B 200 29.986 34.539 26.414 1.00 41.62 B O ATOM 3027 N ASP B 201 30.544 34.405 28.594 1.00 37.35 B N ATOM 3028 CA ASP B 201 31.047 33.043 28.486 1.00 38.32 B C ATOM 3029 CB ASP B 201 31.860 32.688 29.732 1.00 41.37 B C ATOM 3030 CG ASP B 201 33.095 33.570 29.900 1.00 48.78 B C ATOM 3031 OD1 ASP B 201 33.361 34.433 29.024 1.00 45.25 B O ATOM 3032 OD2 ASP B 201 33.809 33.394 30.914 1.00 49.28 B O ATOM 3033 C ASP B 201 29.915 32.035 28.263 1.00 43.29 B C ATOM 3034 O ASP B 201 28.756 32.290 28.624 1.00 43.73 B O ATOM 3035 N ALA B 202 30.244 30.897 27.658 1.00 38.47 B N ATOM 3036 CA ALA B 202 29.250 29.858 27.403 1.00 36.74 B C ATOM 3037 CB ALA B 202 28.935 29.776 25.922 1.00 29.17 B C ATOM 3038 C ALA B 202 29.730 28.512 27.924 1.00 40.02 B C ATOM 3039 O ALA B 202 30.844 28.095 27.638 1.00 44.61 B O ATOM 3040 N HIS B 203 28.886 27.836 28.693 1.00 40.81 B N ATOM 3041 CA HIS B 203 29.251 26.549 29.282 1.00 43.85 B C ATOM 3042 CB HIS B 203 29.166 26.624 30.808 1.00 46.78 B C ATOM 3043 CG HIS B 203 29.981 27.731 31.393 1.00 45.40 B C ATOM 3044 CD2 HIS B 203 31.289 28.043 31.251 1.00 41.37 B C ATOM 3045 ND1 HIS B 203 29.446 28.694 32.220 1.00 53.35 B N ATOM 3046 CE1 HIS B 203 30.394 29.541 32.575 1.00 51.53 B C ATOM 3047 NE2 HIS B 203 31.521 29.170 31.998 1.00 46.70 B N ATOM 3048 C HIS B 203 28.384 25.406 28.787 1.00 42.10 B C ATOM 3049 O HIS B 203 27.216 25.593 28.455 1.00 44.90 B O ATOM 3050 N PHE B 204 28.955 24.212 28.761 1.00 37.02 B N ATOM 3051 CA PHE B 204 28.222 23.047 28.302 1.00 38.68 B C ATOM 3052 CB PHE B 204 28.688 22.632 26.895 1.00 40.39 B C ATOM 3053 CG PHE B 204 28.461 23.692 25.842 1.00 37.67 B C ATOM 3054 CD1 PHE B 204 29.397 24.684 25.624 1.00 36.11 B C ATOM 3055 CD2 PHE B 204 27.303 23.699 25.083 1.00 39.00 B C ATOM 3056 CE1 PHE B 204 29.184 25.660 24.666 1.00 40.74 B C ATOM 3057 CE2 PHE B 204 27.087 24.670 24.123 1.00 37.97 B C ATOM 3058 CZ PHE B 204 28.030 25.654 23.914 1.00 33.23 B C ATOM 3059 C PHE B 204 28.370 21.901 29.297 1.00 44.24 B C ATOM 3060 O PHE B 204 29.444 21.678 29.861 1.00 46.75 B O ATOM 3061 N ASP B 205 27.277 21.180 29.500 1.00 42.07 B N ATOM 3062 CA ASP B 205 27.213 20.107 30.473 1.00 39.94 B C ATOM 3063 CB ASP B 205 25.754 19.861 30.832 1.00 44.47 B C ATOM 3064 CG ASP B 205 25.596 19.097 32.115 1.00 49.98 B C ATOM 3065 OD1 ASP B 205 26.599 18.559 32.632 1.00 52.52 B O ATOM 3066 OD2 ASP B 205 24.461 19.037 32.612 1.00 50.05 B O ATOM 3067 C ASP B 205 27.841 18.821 29.949 1.00 42.30 B C ATOM 3068 O ASP B 205 27.211 18.071 29.209 1.00 44.89 B O ATOM 3069 N ASP B 206 29.079 18.561 30.352 1.00 46.34 B N ATOM 3070 CA ASP B 206 29.852 17.433 29.832 1.00 42.86 B C ATOM 3071 CB ASP B 206 31.315 17.552 30.294 1.00 48.42 B C ATOM 3072 CG ASP B 206 32.323 17.051 29.255 1.00 49.06 B C ATOM 3073 OD1 ASP B 206 31.908 16.570 28.178 1.00 48.20 B O ATOM 3074 OD2 ASP B 206 33.543 17.149 29.523 1.00 41.40 B O ATOM 3075 C ASP B 206 29.227 16.119 30.304 1.00 42.47 B C ATOM 3076 O ASP B 206 29.738 15.038 30.043 1.00 48.03 B O ATOM 3077 N ASP B 207 28.115 16.225 31.016 1.00 47.39 B N ATOM 3078 CA ASP B 207 27.352 15.056 31.423 1.00 49.53 B C ATOM 3079 CB ASP B 207 26.543 15.365 32.676 1.00 42.81 B C ATOM 3080 CG ASP B 207 27.291 15.019 33.937 1.00 53.26 B C ATOM 3081 OD1 ASP B 207 28.130 14.090 33.884 1.00 52.09 B O ATOM 3082 OD2 ASP B 207 27.043 15.671 34.978 1.00 60.99 B O ATOM 3083 C ASP B 207 26.436 14.617 30.291 1.00 48.77 B C ATOM 3084 O ASP B 207 25.770 13.582 30.361 1.00 43.44 B O ATOM 3085 N GLU B 208 26.401 15.431 29.248 1.00 46.40 B N ATOM 3086 CA GLU B 208 25.649 15.094 28.061 1.00 48.70 B C ATOM 3087 CB GLU B 208 25.062 16.354 27.417 1.00 52.00 B C ATOM 3088 CG GLU B 208 24.356 17.262 28.392 1.00 42.41 B C ATOM 3089 CD GLU B 208 23.207 16.572 29.072 1.00 47.16 B C ATOM 3090 OE1 GLU B 208 22.934 15.397 28.751 1.00 42.31 B O ATOM 3091 OE2 GLU B 208 22.574 17.208 29.930 1.00 48.75 B O ATOM 3092 C GLU B 208 26.581 14.402 27.090 1.00 44.42 B C ATOM 3093 O GLU B 208 27.790 14.624 27.111 1.00 44.16 B O ATOM 3094 N LEU B 209 26.007 13.545 26.258 1.00 46.53 B N ATOM 3095 CA LEU B 209 26.733 12.905 25.177 1.00 53.79 B C ATOM 3096 CB LEU B 209 26.104 11.545 24.869 1.00 54.25 B C ATOM 3097 CG LEU B 209 26.417 10.824 23.559 1.00 53.46 B C ATOM 3098 CD1 LEU B 209 27.911 10.607 23.394 1.00 53.00 B C ATOM 3099 CD2 LEU B 209 25.676 9.500 23.537 1.00 63.51 B C ATOM 3100 C LEU B 209 26.626 13.832 23.981 1.00 48.56 B C ATOM 3101 O LEU B 209 25.564 13.930 23.369 1.00 51.30 B O ATOM 3102 N TRP B 210 27.716 14.528 23.668 1.00 42.56 B N ATOM 3103 CA TRP B 210 27.653 15.641 22.729 1.00 44.71 B C ATOM 3104 CB TRP B 210 28.543 16.804 23.202 1.00 41.10 B C ATOM 3105 CG TRP B 210 27.918 17.609 24.323 1.00 44.96 B C ATOM 3106 CD2 TRP B 210 26.806 18.518 24.219 1.00 40.37 B C ATOM 3107 CE2 TRP B 210 26.559 19.027 25.512 1.00 39.93 B C ATOM 3108 CE3 TRP B 210 26.001 18.950 23.158 1.00 37.00 B C ATOM 3109 CD1 TRP B 210 28.280 17.602 25.645 1.00 46.51 B C ATOM 3110 NE1 TRP B 210 27.468 18.455 26.364 1.00 39.55 B N ATOM 3111 CZ2 TRP B 210 25.545 19.948 25.767 1.00 41.79 B C ATOM 3112 CZ3 TRP B 210 24.998 19.857 23.414 1.00 35.63 B C ATOM 3113 CH2 TRP B 210 24.778 20.349 24.707 1.00 41.96 B C ATOM 3114 C TRP B 210 27.975 15.213 21.300 1.00 42.85 B C ATOM 3115 O TRP B 210 29.114 14.891 20.988 1.00 53.27 B O ATOM 3116 N SER B 211 26.956 15.199 20.444 1.00 41.74 B N ATOM 3117 CA SER B 211 27.097 14.729 19.068 1.00 48.75 B C ATOM 3118 CB SER B 211 26.346 13.414 18.883 1.00 50.22 B C ATOM 3119 OG SER B 211 24.975 13.651 18.634 1.00 56.94 B O ATOM 3120 C SER B 211 26.600 15.775 18.064 1.00 48.23 B C ATOM 3121 O SER B 211 26.506 16.954 18.394 1.00 50.52 B O ATOM 3122 N LEU B 212 26.285 15.360 16.842 1.00 47.17 B N ATOM 3123 CA LEU B 212 25.782 16.319 15.862 1.00 49.28 B C ATOM 3124 CB LEU B 212 26.675 16.372 14.629 1.00 50.08 B C ATOM 3125 CG LEU B 212 27.977 17.107 14.935 1.00 56.52 B C ATOM 3126 CD1 LEU B 212 28.742 17.421 13.646 1.00 45.05 B C ATOM 3127 CD2 LEU B 212 27.701 18.379 15.740 1.00 40.62 B C ATOM 3128 C LEU B 212 24.315 16.119 15.484 1.00 55.23 B C ATOM 3129 O LEU B 212 23.937 16.254 14.315 1.00 49.99 B O ATOM 3130 N GLY B 213 23.507 15.819 16.503 1.00 58.43 B N ATOM 3131 CA GLY B 213 22.058 15.775 16.400 1.00 56.98 B C ATOM 3132 C GLY B 213 21.510 14.495 15.812 1.00 58.81 B C ATOM 3133 O GLY B 213 21.113 13.586 16.539 1.00 69.17 B O ATOM 3134 N LYS B 389 21.508 14.454 14.484 1.00 56.84 B N ATOM 3135 CA LYS B 389 21.175 13.290 13.654 1.00 63.38 B C ATOM 3136 CB LYS B 389 22.359 13.005 12.725 1.00 64.52 B C ATOM 3137 CG LYS B 389 23.706 13.534 13.249 1.00 66.09 B C ATOM 3138 CD LYS B 389 24.064 12.983 14.628 1.00 59.33 B C ATOM 3139 CE LYS B 389 25.050 11.837 14.532 1.00 65.09 B C ATOM 3140 NZ LYS B 389 26.283 12.203 13.771 1.00 68.86 B N ATOM 3141 C LYS B 389 20.728 11.956 14.282 1.00 72.00 B C ATOM 3142 O LYS B 389 21.012 10.902 13.720 1.00 66.08 B O ATOM 3143 N GLY B 390 20.013 11.967 15.400 1.00 69.67 B N ATOM 3144 CA GLY B 390 19.585 10.702 15.964 1.00 69.49 B C ATOM 3145 C GLY B 390 19.666 10.521 17.467 1.00 70.68 B C ATOM 3146 O GLY B 390 18.648 10.230 18.090 1.00 73.30 B O ATOM 3147 N GLN B 391 20.848 10.647 18.065 1.00 65.22 B N ATOM 3148 CA GLN B 391 20.932 10.334 19.498 1.00 75.23 B C ATOM 3149 CB GLN B 391 21.304 8.860 19.734 1.00 72.31 B C ATOM 3150 CG GLN B 391 22.394 8.661 20.768 1.00 74.64 B C ATOM 3151 CD GLN B 391 23.762 8.762 20.115 1.00 77.26 B C ATOM 3152 OE1 GLN B 391 23.907 8.397 18.964 1.00 72.38 B O ATOM 3153 NE2 GLN B 391 24.762 9.235 20.840 1.00 81.11 B N ATOM 3154 C GLN B 391 21.723 11.269 20.429 1.00 74.42 B C ATOM 3155 O GLN B 391 21.550 11.214 21.644 1.00 82.25 B O ATOM 3156 N GLY B 392 22.565 12.137 19.888 1.00 66.64 B N ATOM 3157 CA GLY B 392 23.223 13.111 20.741 1.00 56.19 B C ATOM 3158 C GLY B 392 22.435 14.404 20.847 1.00 50.71 B C ATOM 3159 O GLY B 392 21.445 14.585 20.141 1.00 53.71 B O ATOM 3160 N TYR B 393 22.853 15.294 21.744 1.00 45.50 B N ATOM 3161 CA TYR B 393 22.453 16.694 21.636 1.00 46.89 B C ATOM 3162 CB TYR B 393 22.486 17.423 22.985 1.00 41.47 B C ATOM 3163 CG TYR B 393 21.450 16.943 23.970 1.00 43.93 B C ATOM 3164 CD1 TYR B 393 20.092 16.991 23.664 1.00 46.41 B C ATOM 3165 CE1 TYR B 393 19.138 16.552 24.565 1.00 50.23 B C ATOM 3166 CD2 TYR B 393 21.824 16.452 25.210 1.00 44.54 B C ATOM 3167 CE2 TYR B 393 20.880 16.010 26.114 1.00 53.01 B C ATOM 3168 CZ TYR B 393 19.538 16.062 25.788 1.00 52.60 B C ATOM 3169 OH TYR B 393 18.599 15.622 26.692 1.00 50.57 B O ATOM 3170 C TYR B 393 23.425 17.351 20.672 1.00 46.96 B C ATOM 3171 O TYR B 393 24.641 17.273 20.864 1.00 47.65 B O ATOM 3172 N SER B 394 22.897 17.972 19.624 1.00 39.54 B N ATOM 3173 CA SER B 394 23.754 18.633 18.650 1.00 42.93 B C ATOM 3174 CB SER B 394 22.959 19.052 17.411 1.00 40.14 B C ATOM 3175 OG SER B 394 23.627 20.076 16.700 1.00 37.74 B O ATOM 3176 C SER B 394 24.443 19.837 19.282 1.00 42.72 B C ATOM 3177 O SER B 394 23.813 20.862 19.552 1.00 40.19 B O ATOM 3178 N LEU B 395 25.739 19.698 19.529 1.00 40.04 B N ATOM 3179 CA LEU B 395 26.536 20.804 20.027 1.00 35.99 B C ATOM 3180 CB LEU B 395 28.016 20.413 20.114 1.00 36.46 B C ATOM 3181 CG LEU B 395 29.004 21.385 20.778 1.00 40.88 B C ATOM 3182 CD1 LEU B 395 28.684 21.610 22.246 1.00 31.61 B C ATOM 3183 CD2 LEU B 395 30.457 20.905 20.617 1.00 38.79 B C ATOM 3184 C LEU B 395 26.346 21.989 19.102 1.00 36.37 B C ATOM 3185 O LEU B 395 26.337 23.138 19.541 1.00 39.00 B O ATOM 3186 N PHE B 396 26.176 21.712 17.813 1.00 40.97 B N ATOM 3187 CA PHE B 396 25.982 22.797 16.860 1.00 39.88 B C ATOM 3188 CB PHE B 396 25.865 22.284 15.422 1.00 34.67 B C ATOM 3189 CG PHE B 396 25.449 23.347 14.439 1.00 34.50 B C ATOM 3190 CD1 PHE B 396 26.146 24.540 14.350 1.00 33.57 B C ATOM 3191 CD2 PHE B 396 24.366 23.154 13.601 1.00 32.03 B C ATOM 3192 CE1 PHE B 396 25.766 25.521 13.453 1.00 32.32 B C ATOM 3193 CE2 PHE B 396 23.988 24.137 12.702 1.00 26.92 B C ATOM 3194 CZ PHE B 396 24.686 25.323 12.634 1.00 24.31 B C ATOM 3195 C PHE B 396 24.775 23.659 17.239 1.00 36.24 B C ATOM 3196 O PHE B 396 24.920 24.858 17.427 1.00 34.67 B O ATOM 3197 N LEU B 397 23.599 23.035 17.357 1.00 41.03 B N ATOM 3198 CA LEU B 397 22.356 23.728 17.712 1.00 36.24 B C ATOM 3199 CB LEU B 397 21.159 22.772 17.640 1.00 38.19 B C ATOM 3200 CG LEU B 397 20.795 22.196 16.267 1.00 36.80 B C ATOM 3201 CD1 LEU B 397 19.691 21.161 16.372 1.00 31.44 B C ATOM 3202 CD2 LEU B 397 20.405 23.294 15.292 1.00 30.95 B C ATOM 3203 C LEU B 397 22.412 24.366 19.100 1.00 35.79 B C ATOM 3204 O LEU B 397 22.092 25.539 19.259 1.00 37.11 B O ATOM 3205 N VAL B 398 22.820 23.599 20.105 1.00 31.08 B N ATOM 3206 CA VAL B 398 22.888 24.129 21.462 1.00 33.81 B C ATOM 3207 CB VAL B 398 23.380 23.084 22.478 1.00 38.37 B C ATOM 3208 CG1 VAL B 398 23.483 23.715 23.852 1.00 34.21 B C ATOM 3209 CG2 VAL B 398 22.448 21.880 22.509 1.00 38.52 B C ATOM 3210 C VAL B 398 23.791 25.357 21.561 1.00 38.89 B C ATOM 3211 O VAL B 398 23.507 26.282 22.329 1.00 37.30 B O ATOM 3212 N ALA B 399 24.881 25.364 20.795 1.00 38.51 B N ATOM 3213 CA ALA B 399 25.844 26.456 20.879 1.00 31.43 B C ATOM 3214 CB ALA B 399 27.173 26.038 20.372 1.00 26.45 B C ATOM 3215 C ALA B 399 25.364 27.712 20.167 1.00 36.92 B C ATOM 3216 O ALA B 399 25.670 28.823 20.597 1.00 38.41 B O ATOM 3217 N ALA B 400 24.613 27.546 19.084 1.00 35.39 B N ATOM 3218 CA ALA B 400 24.043 28.695 18.393 1.00 35.17 B C ATOM 3219 CB ALA B 400 23.318 28.252 17.134 1.00 35.09 B C ATOM 3220 C ALA B 400 23.079 29.382 19.349 1.00 35.41 B C ATOM 3221 O ALA B 400 23.059 30.604 19.486 1.00 31.98 B O ATOM 3222 N HIS B 401 22.278 28.567 20.018 1.00 39.25 B N ATOM 3223 CA HIS B 401 21.346 29.059 21.002 1.00 32.50 B C ATOM 3224 CB HIS B 401 20.632 27.896 21.679 1.00 32.17 B C ATOM 3225 CG HIS B 401 19.697 28.325 22.764 1.00 41.47 B C ATOM 3226 CD2 HIS B 401 19.869 28.416 24.107 1.00 34.97 B C ATOM 3227 ND1 HIS B 401 18.408 28.745 22.516 1.00 36.12 B N ATOM 3228 CE1 HIS B 401 17.827 29.075 23.655 1.00 37.71 B C ATOM 3229 NE2 HIS B 401 18.692 28.877 24.635 1.00 31.29 B N ATOM 3230 C HIS B 401 22.088 29.868 22.037 1.00 33.21 B C ATOM 3231 O HIS B 401 21.750 31.026 22.291 1.00 34.58 B O ATOM 3232 N GLU B 402 23.113 29.261 22.624 1.00 30.01 B N ATOM 3233 CA GLU B 402 23.811 29.881 23.747 1.00 35.43 B C ATOM 3234 CB GLU B 402 24.811 28.915 24.388 1.00 34.71 B C ATOM 3235 CG GLU B 402 24.177 27.680 25.029 1.00 34.73 B C ATOM 3236 CD GLU B 402 23.178 27.990 26.151 1.00 33.30 B C ATOM 3237 OE1 GLU B 402 23.081 29.151 26.623 1.00 30.76 B O ATOM 3238 OE2 GLU B 402 22.487 27.041 26.560 1.00 30.26 B O ATOM 3239 C GLU B 402 24.515 31.160 23.353 1.00 33.90 B C ATOM 3240 O GLU B 402 24.506 32.137 24.102 1.00 30.46 B O ATOM 3241 N PHE B 403 25.127 31.143 22.171 1.00 39.51 B N ATOM 3242 CA PHE B 403 25.824 32.308 21.656 1.00 31.16 B C ATOM 3243 CB PHE B 403 26.564 31.966 20.374 1.00 35.97 B C ATOM 3244 CG PHE B 403 27.678 30.974 20.578 1.00 38.74 B C ATOM 3245 CD1 PHE B 403 28.127 30.676 21.863 1.00 35.53 B C ATOM 3246 CD2 PHE B 403 28.287 30.352 19.496 1.00 33.75 B C ATOM 3247 CE1 PHE B 403 29.156 29.767 22.066 1.00 31.46 B C ATOM 3248 CE2 PHE B 403 29.318 29.443 19.690 1.00 37.79 B C ATOM 3249 CZ PHE B 403 29.754 29.149 20.980 1.00 36.46 B C ATOM 3250 C PHE B 403 24.847 33.453 21.464 1.00 35.76 B C ATOM 3251 O PHE B 403 25.217 34.617 21.604 1.00 37.98 B O ATOM 3252 N GLY B 404 23.592 33.117 21.182 1.00 35.10 B N ATOM 3253 CA GLY B 404 22.513 34.090 21.255 1.00 34.26 B C ATOM 3254 C GLY B 404 22.497 34.824 22.590 1.00 31.93 B C ATOM 3255 O GLY B 404 22.547 36.050 22.636 1.00 33.08 B O ATOM 3256 N HIS B 405 22.427 34.070 23.682 1.00 36.06 B N ATOM 3257 CA HIS B 405 22.444 34.658 25.022 1.00 33.87 B C ATOM 3258 CB HIS B 405 22.427 33.579 26.110 1.00 33.91 B C ATOM 3259 CG HIS B 405 21.082 32.963 26.353 1.00 35.71 B C ATOM 3260 CD2 HIS B 405 20.731 31.709 26.721 1.00 35.18 B C ATOM 3261 ND1 HIS B 405 19.906 33.679 26.272 1.00 35.49 B N ATOM 3262 CE1 HIS B 405 18.889 32.887 26.554 1.00 34.91 B C ATOM 3263 NE2 HIS B 405 19.360 31.685 26.831 1.00 31.91 B N ATOM 3264 C HIS B 405 23.692 35.495 25.195 1.00 37.58 B C ATOM 3265 O HIS B 405 23.649 36.568 25.788 1.00 33.80 B O ATOM 3266 N ALA B 406 24.806 34.984 24.668 1.00 39.66 B N ATOM 3267 CA ALA B 406 26.118 35.583 24.877 1.00 33.05 B C ATOM 3268 CB ALA B 406 27.204 34.634 24.428 1.00 34.65 B C ATOM 3269 C ALA B 406 26.234 36.916 24.148 1.00 40.07 B C ATOM 3270 O ALA B 406 27.136 37.719 24.422 1.00 39.35 B O ATOM 3271 N LEU B 407 25.321 37.145 23.210 1.00 39.74 B N ATOM 3272 CA LEU B 407 25.255 38.425 22.522 1.00 38.43 B C ATOM 3273 CB LEU B 407 24.874 38.239 21.062 1.00 35.77 B C ATOM 3274 CG LEU B 407 25.812 37.334 20.282 1.00 31.26 B C ATOM 3275 CD1 LEU B 407 25.349 37.260 18.866 1.00 34.69 B C ATOM 3276 CD2 LEU B 407 27.210 37.869 20.356 1.00 35.59 B C ATOM 3277 C LEU B 407 24.241 39.319 23.199 1.00 34.60 B C ATOM 3278 O LEU B 407 24.104 40.475 22.845 1.00 34.18 B O ATOM 3279 N GLY B 408 23.526 38.772 24.174 1.00 37.84 B N ATOM 3280 CA GLY B 408 22.543 39.546 24.909 1.00 37.26 B C ATOM 3281 C GLY B 408 21.108 39.315 24.470 1.00 32.91 B C ATOM 3282 O GLY B 408 20.272 40.212 24.555 1.00 33.74 B O ATOM 3283 N LEU B 409 20.811 38.111 23.996 1.00 32.97 B N ATOM 3284 CA LEU B 409 19.427 37.752 23.703 1.00 33.68 B C ATOM 3285 CB LEU B 409 19.340 36.922 22.428 1.00 41.86 B C ATOM 3286 CG LEU B 409 19.618 37.654 21.117 1.00 40.08 B C ATOM 3287 CD1 LEU B 409 19.484 36.675 19.964 1.00 36.51 B C ATOM 3288 CD2 LEU B 409 18.674 38.851 20.953 1.00 25.32 B C ATOM 3289 C LEU B 409 18.801 36.982 24.852 1.00 36.03 B C ATOM 3290 O LEU B 409 19.496 36.308 25.611 1.00 36.21 B O ATOM 3291 N ASP B 410 17.483 37.101 24.978 1.00 43.30 B N ATOM 3292 CA ASP B 410 16.709 36.344 25.957 1.00 39.82 B C ATOM 3293 CB ASP B 410 15.706 37.253 26.661 1.00 39.96 B C ATOM 3294 CG ASP B 410 16.352 38.094 27.738 1.00 54.39 B C ATOM 3295 OD1 ASP B 410 17.135 37.520 28.536 1.00 56.41 B O ATOM 3296 OD2 ASP B 410 16.083 39.319 27.782 1.00 46.72 B O ATOM 3297 C ASP B 410 15.974 35.231 25.250 1.00 36.56 B C ATOM 3298 O ASP B 410 15.970 35.166 24.029 1.00 38.09 B O ATOM 3299 N HIS B 411 15.339 34.351 26.001 1.00 39.84 B N ATOM 3300 CA HIS B 411 14.574 33.305 25.345 1.00 42.76 B C ATOM 3301 CB HIS B 411 14.089 32.260 26.334 1.00 44.29 B C ATOM 3302 CG HIS B 411 15.164 31.330 26.776 1.00 40.72 B C ATOM 3303 CD2 HIS B 411 15.989 30.530 26.066 1.00 38.93 B C ATOM 3304 ND1 HIS B 411 15.525 31.184 28.096 1.00 41.16 B N ATOM 3305 CE1 HIS B 411 16.512 30.314 28.184 1.00 37.40 B C ATOM 3306 NE2 HIS B 411 16.810 29.900 26.966 1.00 40.78 B N ATOM 3307 C HIS B 411 13.408 33.860 24.555 1.00 45.16 B C ATOM 3308 O HIS B 411 13.057 35.034 24.672 1.00 44.14 B O ATOM 3309 N SER B 412 12.816 32.976 23.762 1.00 44.46 B N ATOM 3310 CA SER B 412 11.753 33.297 22.827 1.00 38.92 B C ATOM 3311 CB SER B 412 12.223 32.895 21.422 1.00 32.94 B C ATOM 3312 OG SER B 412 11.250 33.144 20.428 1.00 29.52 B O ATOM 3313 C SER B 412 10.488 32.516 23.223 1.00 38.77 B C ATOM 3314 O SER B 412 10.578 31.420 23.788 1.00 37.31 B O ATOM 3315 N SER B 413 9.310 33.064 22.939 1.00 35.12 B N ATOM 3316 CA SER B 413 8.086 32.290 23.150 1.00 35.56 B C ATOM 3317 CB SER B 413 6.948 33.130 23.749 1.00 37.57 B C ATOM 3318 OG SER B 413 6.708 34.318 23.028 1.00 42.13 B O ATOM 3319 C SER B 413 7.647 31.554 21.891 1.00 38.41 B C ATOM 3320 O SER B 413 6.968 30.535 21.972 1.00 48.24 B O ATOM 3321 N VAL B 414 8.060 32.055 20.731 1.00 40.19 B N ATOM 3322 CA VAL B 414 7.835 31.349 19.469 1.00 39.61 B C ATOM 3323 CB VAL B 414 8.314 32.172 18.253 1.00 34.60 B C ATOM 3324 CG1 VAL B 414 8.171 31.359 16.958 1.00 32.12 B C ATOM 3325 CG2 VAL B 414 7.541 33.480 18.172 1.00 25.42 B C ATOM 3326 C VAL B 414 8.553 30.009 19.485 1.00 38.87 B C ATOM 3327 O VAL B 414 9.776 29.959 19.520 1.00 44.42 B O ATOM 3328 N PRO B 415 7.788 28.914 19.453 1.00 44.19 B N ATOM 3329 CD PRO B 415 6.329 28.902 19.271 1.00 42.97 B C ATOM 3330 CA PRO B 415 8.334 27.563 19.622 1.00 44.37 B C ATOM 3331 CB PRO B 415 7.128 26.655 19.362 1.00 40.20 B C ATOM 3332 CG PRO B 415 5.955 27.504 19.669 1.00 44.24 B C ATOM 3333 C PRO B 415 9.457 27.229 18.656 1.00 43.10 B C ATOM 3334 O PRO B 415 10.465 26.697 19.104 1.00 47.86 B O ATOM 3335 N GLU B 416 9.299 27.518 17.367 1.00 45.13 B N ATOM 3336 CA GLU B 416 10.288 27.050 16.384 1.00 54.15 B C ATOM 3337 CB GLU B 416 9.669 26.828 14.992 1.00 50.62 B C ATOM 3338 CG GLU B 416 8.511 27.747 14.660 1.00 56.34 B C ATOM 3339 CD GLU B 416 7.278 27.412 15.463 1.00 57.77 B C ATOM 3340 OE1 GLU B 416 7.257 26.311 16.056 1.00 56.98 B O ATOM 3341 OE2 GLU B 416 6.338 28.240 15.504 1.00 56.48 B O ATOM 3342 C GLU B 416 11.549 27.910 16.283 1.00 47.24 B C ATOM 3343 O GLU B 416 12.517 27.506 15.639 1.00 44.81 B O ATOM 3344 N ALA B 417 11.535 29.080 16.923 1.00 45.05 B N ATOM 3345 CA ALA B 417 12.703 29.965 16.945 1.00 45.26 B C ATOM 3346 CB ALA B 417 12.363 31.290 17.620 1.00 35.21 B C ATOM 3347 C ALA B 417 13.893 29.308 17.643 1.00 40.79 B C ATOM 3348 O ALA B 417 13.718 28.486 18.538 1.00 38.86 B O ATOM 3349 N LEU B 418 15.099 29.686 17.231 1.00 37.49 B N ATOM 3350 CA LEU B 418 16.328 29.141 17.809 1.00 42.61 B C ATOM 3351 CB LEU B 418 17.547 29.671 17.049 1.00 33.35 B C ATOM 3352 CG LEU B 418 18.889 29.419 17.741 1.00 33.33 B C ATOM 3353 CD1 LEU B 418 19.255 27.943 17.664 1.00 32.39 B C ATOM 3354 CD2 LEU B 418 19.986 30.280 17.145 1.00 32.37 B C ATOM 3355 C LEU B 418 16.489 29.423 19.316 1.00 38.41 B C ATOM 3356 O LEU B 418 16.987 28.582 20.067 1.00 31.04 B O ATOM 3357 N MET B 419 16.089 30.620 19.732 1.00 38.69 B N ATOM 3358 CA MET B 419 16.199 31.057 21.120 1.00 34.98 B C ATOM 3359 CB MET B 419 16.323 32.576 21.183 1.00 29.60 B C ATOM 3360 CG MET B 419 17.549 33.124 20.486 1.00 28.78 B C ATOM 3361 SD MET B 419 19.068 32.447 21.162 1.00 31.82 B S ATOM 3362 CE MET B 419 18.776 32.618 22.928 1.00 31.73 B C ATOM 3363 C MET B 419 14.986 30.604 21.925 1.00 41.43 B C ATOM 3364 O MET B 419 14.568 31.265 22.870 1.00 45.23 B O ATOM 3365 N TYR B 420 14.406 29.484 21.518 1.00 41.58 B N ATOM 3366 CA TYR B 420 13.392 28.822 22.303 1.00 38.95 B C ATOM 3367 CB TYR B 420 12.611 27.862 21.422 1.00 37.97 B C ATOM 3368 CG TYR B 420 11.312 27.400 22.019 1.00 46.04 B C ATOM 3369 CD1 TYR B 420 10.303 28.309 22.335 1.00 44.66 B C ATOM 3370 CE1 TYR B 420 9.103 27.881 22.876 1.00 43.67 B C ATOM 3371 CD2 TYR B 420 11.081 26.053 22.263 1.00 49.41 B C ATOM 3372 CE2 TYR B 420 9.883 25.619 22.804 1.00 46.00 B C ATOM 3373 CZ TYR B 420 8.901 26.534 23.106 1.00 41.79 B C ATOM 3374 OH TYR B 420 7.717 26.095 23.648 1.00 45.79 B O ATOM 3375 C TYR B 420 14.148 28.045 23.356 1.00 39.98 B C ATOM 3376 O TYR B 420 15.175 27.447 23.054 1.00 42.50 B O ATOM 3377 N PRO B 421 13.646 28.046 24.598 1.00 45.27 B N ATOM 3378 CD PRO B 421 12.382 28.673 25.022 1.00 42.84 B C ATOM 3379 CA PRO B 421 14.357 27.413 25.717 1.00 41.10 B C ATOM 3380 CB PRO B 421 13.445 27.699 26.917 1.00 42.46 B C ATOM 3381 CG PRO B 421 12.568 28.835 26.494 1.00 42.41 B C ATOM 3382 C PRO B 421 14.542 25.901 25.556 1.00 42.27 B C ATOM 3383 O PRO B 421 15.502 25.342 26.090 1.00 43.29 B O ATOM 3384 N MET B 422 13.633 25.244 24.845 1.00 39.49 B N ATOM 3385 CA MET B 422 13.668 23.789 24.761 1.00 41.29 B C ATOM 3386 CB MET B 422 12.278 23.225 24.521 1.00 53.64 B C ATOM 3387 CG MET B 422 11.306 23.468 25.636 1.00 46.99 B C ATOM 3388 SD MET B 422 9.818 22.532 25.304 1.00 59.92 B S ATOM 3389 CE MET B 422 8.827 23.022 26.711 1.00 52.65 B C ATOM 3390 C MET B 422 14.559 23.342 23.642 1.00 42.87 B C ATOM 3391 O MET B 422 14.816 24.101 22.714 1.00 54.09 B O ATOM 3392 N TYR B 423 15.013 22.097 23.712 1.00 47.02 B N ATOM 3393 CA TYR B 423 15.942 21.586 22.710 1.00 50.60 B C ATOM 3394 CB TYR B 423 16.919 20.578 23.314 1.00 45.12 B C ATOM 3395 CG TYR B 423 17.713 19.850 22.255 1.00 45.67 B C ATOM 3396 CD1 TYR B 423 17.311 18.604 21.795 1.00 46.09 B C ATOM 3397 CE1 TYR B 423 18.022 17.939 20.815 1.00 44.01 B C ATOM 3398 CD2 TYR B 423 18.848 20.421 21.694 1.00 41.38 B C ATOM 3399 CE2 TYR B 423 19.568 19.760 20.715 1.00 43.51 B C ATOM 3400 CZ TYR B 423 19.149 18.518 20.281 1.00 41.33 B C ATOM 3401 OH TYR B 423 19.859 17.849 19.313 1.00 42.90 B O ATOM 3402 C TYR B 423 15.233 20.952 21.522 1.00 47.44 B C ATOM 3403 O TYR B 423 14.831 19.793 21.575 1.00 50.43 B O ATOM 3404 N ARG B 424 15.087 21.711 20.445 1.00 48.86 B N ATOM 3405 CA ARG B 424 14.528 21.158 19.218 1.00 51.94 B C ATOM 3406 CB ARG B 424 13.524 22.129 18.596 1.00 50.84 B C ATOM 3407 CG ARG B 424 12.703 21.514 17.477 1.00 55.24 B C ATOM 3408 CD ARG B 424 11.591 22.443 16.998 1.00 53.75 B C ATOM 3409 NE ARG B 424 12.056 23.468 16.062 1.00 61.04 B N ATOM 3410 CZ ARG B 424 12.087 23.320 14.737 1.00 65.72 B C ATOM 3411 NH1 ARG B 424 11.693 22.175 14.183 1.00 61.54 B N ATOM 3412 NH2 ARG B 424 12.517 24.314 13.965 1.00 53.10 B N ATOM 3413 C ARG B 424 15.635 20.844 18.218 1.00 43.72 B C ATOM 3414 O ARG B 424 16.232 21.751 17.655 1.00 42.89 B O ATOM 3415 N PHE B 425 15.926 19.566 18.013 1.00 41.31 B N ATOM 3416 CA PHE B 425 16.796 19.186 16.907 1.00 41.48 B C ATOM 3417 CB PHE B 425 17.237 17.730 17.009 1.00 37.91 B C ATOM 3418 CG PHE B 425 17.965 17.249 15.797 1.00 41.35 B C ATOM 3419 CD1 PHE B 425 19.319 17.496 15.643 1.00 44.97 B C ATOM 3420 CD2 PHE B 425 17.295 16.572 14.794 1.00 39.51 B C ATOM 3421 CE1 PHE B 425 19.993 17.074 14.509 1.00 44.66 B C ATOM 3422 CE2 PHE B 425 17.963 16.145 13.662 1.00 44.81 B C ATOM 3423 CZ PHE B 425 19.313 16.396 13.519 1.00 47.96 B C ATOM 3424 C PHE B 425 16.100 19.417 15.564 1.00 38.40 B C ATOM 3425 O PHE B 425 14.935 19.080 15.382 1.00 44.23 B O ATOM 3426 N THR B 426 16.820 20.001 14.626 1.00 38.81 B N ATOM 3427 CA THR B 426 16.291 20.214 13.288 1.00 43.84 B C ATOM 3428 CB THR B 426 15.650 21.618 13.140 1.00 46.19 B C ATOM 3429 OG1 THR B 426 14.864 21.669 11.939 1.00 41.44 B O ATOM 3430 CG2 THR B 426 16.727 22.707 13.102 1.00 37.03 B C ATOM 3431 C THR B 426 17.437 20.056 12.298 1.00 40.21 B C ATOM 3432 O THR B 426 18.591 20.275 12.653 1.00 34.83 B O ATOM 3433 N GLU B 427 17.120 19.647 11.073 1.00 44.75 B N ATOM 3434 CA GLU B 427 18.119 19.538 10.019 1.00 39.86 B C ATOM 3435 CB GLU B 427 17.819 18.357 9.097 1.00 37.66 B C ATOM 3436 CG GLU B 427 17.778 16.993 9.779 1.00 51.55 B C ATOM 3437 CD GLU B 427 19.155 16.360 9.958 1.00 64.43 B C ATOM 3438 OE1 GLU B 427 20.171 16.989 9.572 1.00 62.60 B O ATOM 3439 OE2 GLU B 427 19.218 15.226 10.486 1.00 63.30 B O ATOM 3440 C GLU B 427 18.111 20.827 9.219 1.00 40.92 B C ATOM 3441 O GLU B 427 18.971 21.054 8.364 1.00 45.81 B O ATOM 3442 N GLY B 428 17.132 21.675 9.506 1.00 38.95 B N ATOM 3443 CA GLY B 428 16.924 22.887 8.734 1.00 43.85 B C ATOM 3444 C GLY B 428 17.589 24.120 9.310 1.00 36.99 B C ATOM 3445 O GLY B 428 18.116 24.078 10.423 1.00 36.41 B O ATOM 3446 N PRO B 429 17.556 25.230 8.554 1.00 37.44 B N ATOM 3447 CD PRO B 429 16.822 25.326 7.278 1.00 31.00 B C ATOM 3448 CA PRO B 429 18.234 26.488 8.902 1.00 28.59 B C ATOM 3449 CB PRO B 429 17.753 27.451 7.817 1.00 31.30 B C ATOM 3450 CG PRO B 429 17.380 26.563 6.661 1.00 30.77 B C ATOM 3451 C PRO B 429 17.842 26.987 10.293 1.00 36.22 B C ATOM 3452 O PRO B 429 16.683 27.332 10.532 1.00 35.94 B O ATOM 3453 N PRO B 430 18.812 27.008 11.214 1.00 36.27 B N ATOM 3454 CD PRO B 430 20.174 26.527 10.917 1.00 28.12 B C ATOM 3455 CA PRO B 430 18.646 27.335 12.632 1.00 33.91 B C ATOM 3456 CB PRO B 430 20.092 27.377 13.135 1.00 39.95 B C ATOM 3457 CG PRO B 430 20.797 26.365 12.273 1.00 26.98 B C ATOM 3458 C PRO B 430 17.928 28.660 12.934 1.00 37.72 B C ATOM 3459 O PRO B 430 16.936 28.647 13.662 1.00 35.11 B O ATOM 3460 N LEU B 431 18.419 29.780 12.411 1.00 38.24 B N ATOM 3461 CA LEU B 431 17.819 31.074 12.739 1.00 33.69 B C ATOM 3462 CB LEU B 431 18.637 32.232 12.153 1.00 33.63 B C ATOM 3463 CG LEU B 431 20.042 32.555 12.672 1.00 28.73 B C ATOM 3464 CD1 LEU B 431 20.599 33.734 11.909 1.00 23.36 B C ATOM 3465 CD2 LEU B 431 20.020 32.864 14.155 1.00 31.39 B C ATOM 3466 C LEU B 431 16.385 31.163 12.233 1.00 39.12 B C ATOM 3467 O LEU B 431 16.074 30.676 11.140 1.00 41.93 B O ATOM 3468 N HIS B 432 15.521 31.795 13.027 1.00 39.31 B N ATOM 3469 CA HIS B 432 14.141 32.082 12.625 1.00 37.61 B C ATOM 3470 CB HIS B 432 13.164 31.295 13.490 1.00 36.42 B C ATOM 3471 CG HIS B 432 12.824 29.945 12.945 1.00 36.01 B C ATOM 3472 CD2 HIS B 432 11.752 29.514 12.243 1.00 35.57 B C ATOM 3473 ND1 HIS B 432 13.639 28.845 13.113 1.00 40.00 B N ATOM 3474 CE1 HIS B 432 13.088 27.798 12.530 1.00 34.96 B C ATOM 3475 NE2 HIS B 432 11.938 28.174 12.000 1.00 35.19 B N ATOM 3476 C HIS B 432 13.827 33.591 12.663 1.00 37.35 B C ATOM 3477 O HIS B 432 14.616 34.386 13.186 1.00 33.05 B O ATOM 3478 N LYS B 433 12.686 33.981 12.098 1.00 32.05 B N ATOM 3479 CA LYS B 433 12.347 35.401 11.962 1.00 34.88 B C ATOM 3480 CB LYS B 433 10.919 35.578 11.448 1.00 38.30 B C ATOM 3481 CG LYS B 433 10.759 35.580 9.934 1.00 40.80 B C ATOM 3482 CD LYS B 433 9.279 35.463 9.552 1.00 37.88 B C ATOM 3483 CE LYS B 433 9.061 35.315 8.045 1.00 40.11 B C ATOM 3484 NZ LYS B 433 8.865 36.616 7.344 1.00 38.99 B N ATOM 3485 C LYS B 433 12.501 36.154 13.276 1.00 36.47 B C ATOM 3486 O LYS B 433 12.998 37.282 13.310 1.00 37.47 B O ATOM 3487 N ASP B 434 12.072 35.517 14.359 1.00 38.85 B N ATOM 3488 CA ASP B 434 12.106 36.122 15.684 1.00 33.79 B C ATOM 3489 CB ASP B 434 11.248 35.315 16.665 1.00 34.12 B C ATOM 3490 CG ASP B 434 10.855 36.119 17.890 1.00 39.64 B C ATOM 3491 OD1 ASP B 434 10.412 37.277 17.712 1.00 39.66 B O ATOM 3492 OD2 ASP B 434 10.985 35.596 19.021 1.00 34.25 B O ATOM 3493 C ASP B 434 13.527 36.253 16.219 1.00 33.80 B C ATOM 3494 O ASP B 434 13.846 37.218 16.910 1.00 33.26 B O ATOM 3495 N ASP B 435 14.377 35.276 15.915 1.00 33.33 B N ATOM 3496 CA ASP B 435 15.776 35.376 16.294 1.00 29.72 B C ATOM 3497 CB ASP B 435 16.547 34.141 15.873 1.00 33.76 B C ATOM 3498 CG ASP B 435 15.885 32.866 16.299 1.00 34.51 B C ATOM 3499 OD1 ASP B 435 16.106 32.435 17.444 1.00 39.97 B O ATOM 3500 OD2 ASP B 435 15.159 32.280 15.478 1.00 37.24 B O ATOM 3501 C ASP B 435 16.381 36.596 15.625 1.00 34.00 B C ATOM 3502 O ASP B 435 17.136 37.338 16.239 1.00 43.44 B O ATOM 3503 N VAL B 436 16.041 36.812 14.361 1.00 36.85 B N ATOM 3504 CA VAL B 436 16.614 37.926 13.610 1.00 37.75 B C ATOM 3505 CB VAL B 436 16.300 37.825 12.092 1.00 41.65 B C ATOM 3506 CG1 VAL B 436 16.767 39.066 11.357 1.00 38.72 B C ATOM 3507 CG2 VAL B 436 16.957 36.595 11.502 1.00 37.20 B C ATOM 3508 C VAL B 436 16.145 39.261 14.176 1.00 38.83 B C ATOM 3509 O VAL B 436 16.967 40.122 14.495 1.00 40.16 B O ATOM 3510 N ASN B 437 14.825 39.419 14.300 1.00 41.55 B N ATOM 3511 CA ASN B 437 14.220 40.594 14.935 1.00 37.98 B C ATOM 3512 CB ASN B 437 12.734 40.348 15.228 1.00 39.82 B C ATOM 3513 CG ASN B 437 11.919 40.096 13.971 1.00 41.05 B C ATOM 3514 OD1 ASN B 437 12.342 40.434 12.860 1.00 40.25 B O ATOM 3515 ND2 ASN B 437 10.737 39.499 14.143 1.00 37.66 B N ATOM 3516 C ASN B 437 14.909 40.905 16.240 1.00 33.15 B C ATOM 3517 O ASN B 437 15.405 42.007 16.453 1.00 38.63 B O ATOM 3518 N GLY B 438 14.925 39.914 17.118 1.00 34.30 B N ATOM 3519 CA GLY B 438 15.583 40.037 18.398 1.00 32.90 B C ATOM 3520 C GLY B 438 16.965 40.617 18.251 1.00 33.61 B C ATOM 3521 O GLY B 438 17.221 41.718 18.718 1.00 35.24 B O ATOM 3522 N ILE B 439 17.855 39.882 17.590 1.00 35.36 B N ATOM 3523 CA ILE B 439 19.229 40.340 17.384 1.00 35.59 B C ATOM 3524 CB ILE B 439 20.058 39.323 16.552 1.00 42.62 B C ATOM 3525 CG2 ILE B 439 19.713 39.414 15.076 1.00 37.47 B C ATOM 3526 CG1 ILE B 439 21.558 39.510 16.805 1.00 31.51 B C ATOM 3527 CD1 ILE B 439 21.955 39.222 18.229 1.00 31.55 B C ATOM 3528 C ILE B 439 19.307 41.745 16.761 1.00 38.77 B C ATOM 3529 O ILE B 439 20.010 42.614 17.278 1.00 39.77 B O ATOM 3530 N ARG B 440 18.584 41.973 15.668 1.00 34.96 B N ATOM 3531 CA ARG B 440 18.585 43.291 15.041 1.00 39.46 B C ATOM 3532 CB ARG B 440 17.640 43.337 13.843 1.00 37.61 B C ATOM 3533 CG ARG B 440 18.173 42.662 12.609 1.00 37.83 B C ATOM 3534 CD ARG B 440 17.157 42.741 11.484 1.00 44.10 B C ATOM 3535 NE ARG B 440 17.564 41.946 10.328 1.00 47.73 B N ATOM 3536 CZ ARG B 440 17.054 42.083 9.108 1.00 50.10 B C ATOM 3537 NH1 ARG B 440 16.116 42.994 8.873 1.00 50.41 B N ATOM 3538 NH2 ARG B 440 17.492 41.319 8.117 1.00 46.95 B N ATOM 3539 C ARG B 440 18.213 44.388 16.031 1.00 42.41 B C ATOM 3540 O ARG B 440 18.820 45.453 16.031 1.00 40.63 B O ATOM 3541 N HIS B 441 17.204 44.132 16.861 1.00 41.17 B N ATOM 3542 CA HIS B 441 16.827 45.064 17.922 1.00 42.17 B C ATOM 3543 CB HIS B 441 15.933 44.351 18.940 1.00 45.93 B C ATOM 3544 CG HIS B 441 15.270 45.260 19.929 1.00 53.49 B C ATOM 3545 CD2 HIS B 441 13.985 45.680 20.030 1.00 57.99 B C ATOM 3546 ND1 HIS B 441 15.938 45.815 20.999 1.00 56.29 B N ATOM 3547 CE1 HIS B 441 15.101 46.559 21.701 1.00 54.49 B C ATOM 3548 NE2 HIS B 441 13.909 46.491 21.136 1.00 50.49 B N ATOM 3549 C HIS B 441 18.094 45.595 18.596 1.00 49.37 B C ATOM 3550 O HIS B 441 18.347 46.802 18.603 1.00 52.85 B O ATOM 3551 N LEU B 442 18.902 44.680 19.129 1.00 45.59 B N ATOM 3552 CA LEU B 442 20.158 45.031 19.796 1.00 44.32 B C ATOM 3553 CB LEU B 442 20.831 43.773 20.354 1.00 40.10 B C ATOM 3554 CG LEU B 442 20.560 43.388 21.811 1.00 42.68 B C ATOM 3555 CD1 LEU B 442 19.202 43.882 22.274 1.00 41.57 B C ATOM 3556 CD2 LEU B 442 20.676 41.893 21.986 1.00 36.14 B C ATOM 3557 C LEU B 442 21.162 45.793 18.923 1.00 43.98 B C ATOM 3558 O LEU B 442 21.549 46.919 19.240 1.00 48.51 B O ATOM 3559 N TYR B 443 21.592 45.172 17.831 1.00 44.59 B N ATOM 3560 CA TYR B 443 22.728 45.683 17.076 1.00 38.25 B C ATOM 3561 CB TYR B 443 23.739 44.563 16.843 1.00 44.01 B C ATOM 3562 CG TYR B 443 24.183 43.874 18.111 1.00 40.20 B C ATOM 3563 CD1 TYR B 443 23.657 42.645 18.472 1.00 33.45 B C ATOM 3564 CE1 TYR B 443 24.054 42.014 19.622 1.00 29.70 B C ATOM 3565 CD2 TYR B 443 25.126 44.457 18.948 1.00 37.17 B C ATOM 3566 CE2 TYR B 443 25.527 43.835 20.098 1.00 37.41 B C ATOM 3567 CZ TYR B 443 24.982 42.610 20.430 1.00 37.02 B C ATOM 3568 OH TYR B 443 25.380 41.972 21.581 1.00 45.31 B O ATOM 3569 C TYR B 443 22.360 46.341 15.746 1.00 38.90 B C ATOM 3570 O TYR B 443 23.239 46.736 14.978 1.00 45.23 B O ATOM 3571 N GLY B 444 21.068 46.459 15.473 1.00 35.79 B N ATOM 3572 CA GLY B 444 20.611 47.107 14.258 1.00 35.91 B C ATOM 3573 C GLY B 444 20.677 46.245 13.015 1.00 31.37 B C ATOM 3574 O GLY B 444 19.800 46.341 12.163 1.00 33.15 B O ATOM 3575 ZN ZN B 500 18.805 29.746 26.683 1.00 42.53 B Zn ATOM 3576 ZN ZN B 501 28.409 27.765 34.203 1.00 47.53 B Zn ATOM 3577 CA CA B 502 22.234 18.035 32.429 1.00 56.15 B Ca ATOM 3578 CA CA B 504 34.346 37.370 29.501 1.00 67.64 B Ca ATOM 3579 C01 LIG C 1 23.381 30.840 34.333 1.00 53.33 A C ATOM 3580 O02 LIG C 1 22.683 31.724 33.497 1.00 49.94 A O ATOM 3581 C03 LIG C 1 21.906 32.725 34.058 1.00 50.08 A C ATOM 3582 C04 LIG C 1 21.566 32.691 35.465 1.00 57.59 A C ATOM 3583 C05 LIG C 1 20.725 33.749 36.037 1.00 58.70 A C ATOM 3584 C06 LIG C 1 20.207 34.888 35.143 1.00 64.32 A C ATOM 3585 C07 LIG C 1 20.542 34.923 33.768 1.00 53.68 A C ATOM 3586 C08 LIG C 1 21.404 33.836 33.185 1.00 51.64 A C ATOM 3587 N09 LIG C 1 21.767 33.805 31.741 1.00 47.46 A N ATOM 3588 C10 LIG C 1 21.536 34.934 30.816 1.00 48.02 A C ATOM 3589 N11 LIG C 1 20.680 36.173 31.113 1.00 57.95 A N ATOM 3590 C12 LIG C 1 20.698 37.157 29.760 1.00 58.61 A C ATOM 3591 C13 LIG C 1 21.526 36.525 28.769 1.00 51.23 A C ATOM 3592 S14 LIG C 1 22.088 35.049 29.409 1.00 45.15 A S ATOM 3593 C15 LIG C 1 20.059 38.393 29.702 1.00 55.14 A C ATOM 3594 S16 LIG C 1 19.503 39.228 28.415 1.00 59.20 A S ATOM 3595 C17 LIG C 1 18.848 40.567 28.978 1.00 65.97 A C ATOM 3596 N18 LIG C 1 18.212 41.643 28.212 1.00 58.41 A N ATOM 3597 N19 LIG C 1 18.973 40.566 30.481 1.00 62.23 A N ATOM 3598 C20 LIG C 1 19.749 39.170 30.915 1.00 54.08 A C ATOM 3599 C21 LIG C 1 20.110 38.742 32.348 1.00 59.61 A C ATOM 3600 C22 LIG C 1 19.297 35.964 35.750 1.00 68.76 A C ATOM 3601 N23 LIG C 1 19.723 36.603 36.969 1.00 64.88 A N ATOM 3602 O24 LIG C 1 18.141 35.979 35.457 1.00 64.69 A O END

TABLE 14 Coordinates for proMMP9(35-444 ΔFnII) (SEQ ID NO: 12) complex with Example 4 ATOM 1 N THR A 40 6.815 61.205 26.895 1.00 41.49 A N ATOM 2 CA THR A 40 5.541 61.896 26.714 1.00 44.51 A C ATOM 3 C THR A 40 5.611 62.901 25.558 1.00 48.92 A C ATOM 4 CB THR A 40 5.048 62.568 28.032 1.00 47.93 A C ATOM 5 OG1 THR A 40 4.274 63.743 27.739 1.00 53.72 A O ATOM 6 CG2 THR A 40 6.208 62.952 28.906 1.00 44.24 A C ATOM 7 O THR A 40 6.701 63.190 25.053 1.00 47.24 A O ATOM 8 CB ASP A 41 2.973 64.531 23.474 1.00 40.84 A C ATOM 9 CG ASP A 41 2.408 63.258 22.893 1.00 38.30 A C ATOM 10 OD1 ASP A 41 3.179 62.323 22.615 1.00 37.84 A O ATOM 11 OD2 ASP A 41 1.178 63.197 22.706 1.00 40.04 A O ATOM 12 C ASP A 41 4.883 65.703 24.519 1.00 43.31 A C ATOM 13 O ASP A 41 5.735 66.337 23.896 1.00 38.74 A O ATOM 14 N ASP A 41 4.450 63.393 25.115 1.00 46.41 A N ATOM 15 CA ASP A 41 4.396 64.360 24.016 1.00 44.76 A C ATOM 16 N ARG A 42 4.332 66.125 25.654 1.00 41.84 A N ATOM 17 CA ARG A 42 4.684 67.405 26.244 1.00 41.99 A C ATOM 18 CB ARG A 42 3.732 67.746 27.396 1.00 44.53 A C ATOM 19 CG ARG A 42 4.121 68.991 28.198 1.00 53.97 A C ATOM 20 CD ARG A 42 3.435 70.276 27.713 1.00 50.68 A C ATOM 21 NE ARG A 42 3.990 71.458 28.379 1.00 60.32 A N ATOM 22 CZ ARG A 42 3.356 72.624 28.525 1.00 59.61 A C ATOM 23 NH1 ARG A 42 2.120 72.785 28.061 1.00 51.20 A N ATOM 24 NH2 ARG A 42 3.962 73.634 29.145 1.00 56.54 A N ATOM 25 C ARG A 42 6.154 67.437 26.681 1.00 43.15 A C ATOM 26 O ARG A 42 6.772 68.502 26.715 1.00 46.76 A O ATOM 27 N GLN A 43 6.717 66.268 26.978 1.00 41.55 A N ATOM 28 CA GLN A 43 8.113 66.169 27.395 1.00 40.76 A C ATOM 29 CB GLN A 43 8.368 64.839 28.107 1.00 40.10 A C ATOM 30 CG GLN A 43 9.833 64.402 28.181 1.00 45.45 A C ATOM 31 CD GLN A 43 10.023 63.009 28.796 1.00 50.08 A C ATOM 32 OE1 GLN A 43 9.114 62.174 28.790 1.00 55.94 A O ATOM 33 NE2 GLN A 43 11.216 62.756 29.320 1.00 45.78 A N ATOM 34 C GLN A 43 9.034 66.265 26.193 1.00 41.53 A C ATOM 35 O GLN A 43 10.056 66.951 26.237 1.00 36.67 A O ATOM 36 N LEU A 44 8.674 65.536 25.135 1.00 39.20 A N ATOM 37 CA LEU A 44 9.424 65.531 23.893 1.00 37.68 A C ATOM 38 CB LEU A 44 8.786 64.565 22.890 1.00 39.15 A C ATOM 39 CG LEU A 44 9.020 64.713 21.378 1.00 40.36 A C ATOM 40 CD1 LEU A 44 10.502 64.746 20.999 1.00 41.17 A C ATOM 41 CD2 LEU A 44 8.329 63.588 20.642 1.00 37.97 A C ATOM 42 C LEU A 44 9.488 66.951 23.346 1.00 36.20 A C ATOM 43 O LEU A 44 10.530 67.393 22.870 1.00 37.28 A O ATOM 44 N ALA A 45 8.382 67.676 23.464 1.00 31.95 A N ATOM 45 CA ALA A 45 8.289 69.019 22.912 1.00 32.90 A C ATOM 46 CB ALA A 45 6.847 69.460 22.852 1.00 36.64 A C ATOM 47 C ALA A 45 9.130 70.030 23.690 1.00 38.02 A C ATOM 48 O ALA A 45 9.785 70.895 23.092 1.00 34.03 A O ATOM 49 N GLU A 46 9.104 69.930 25.020 1.00 39.34 A N ATOM 50 CA GLU A 46 9.974 70.757 25.850 1.00 37.95 A C ATOM 51 CB GLU A 46 9.734 70.482 27.341 1.00 37.81 A C ATOM 52 CG GLU A 46 8.416 71.068 27.857 1.00 48.83 A C ATOM 53 CD GLU A 46 8.024 70.601 29.271 1.00 58.46 A C ATOM 54 OE1 GLU A 46 8.888 70.072 30.013 1.00 56.20 A O ATOM 55 OE2 GLU A 46 6.838 70.773 29.638 1.00 60.95 A O ATOM 56 C GLU A 46 11.455 70.552 25.499 1.00 34.76 A C ATOM 57 O GLU A 46 12.212 71.514 25.361 1.00 32.46 A O ATOM 58 N GLU A 47 11.854 69.291 25.377 1.00 30.80 A N ATOM 59 CA GLU A 47 13.216 68.918 25.049 1.00 34.96 A C ATOM 60 CB GLU A 47 13.356 67.399 25.212 1.00 35.72 A C ATOM 61 CG GLU A 47 14.728 66.822 24.970 1.00 42.08 A C ATOM 62 CD GLU A 47 15.779 67.356 25.932 1.00 50.60 A C ATOM 63 OE1 GLU A 47 15.392 67.895 26.994 1.00 52.94 A O ATOM 64 OE2 GLU A 47 16.992 67.239 25.624 1.00 48.16 A O ATOM 65 C GLU A 47 13.589 69.357 23.616 1.00 34.61 A C ATOM 66 O GLU A 47 14.677 69.879 23.371 1.00 35.40 A O ATOM 67 N TYR A 48 12.684 69.139 22.671 1.00 30.60 A N ATOM 68 CA TYR A 48 12.933 69.525 21.286 1.00 31.95 A C ATOM 69 CB TYR A 48 11.777 69.071 20.419 1.00 31.53 A C ATOM 70 CG TYR A 48 12.019 69.102 18.934 1.00 26.09 A C ATOM 71 CD1 TYR A 48 11.919 70.290 18.213 1.00 24.34 A C ATOM 72 CE1 TYR A 48 12.124 70.306 16.825 1.00 27.70 A C ATOM 73 CD2 TYR A 48 12.307 67.929 18.242 1.00 26.24 A C ATOM 74 CE2 TYR A 48 12.504 67.931 16.872 1.00 26.15 A C ATOM 75 CZ TYR A 48 12.416 69.120 16.167 1.00 24.76 A C ATOM 76 OH TYR A 48 12.627 69.110 14.800 1.00 26.92 A O ATOM 77 C TYR A 48 13.101 71.038 21.185 1.00 29.96 A C ATOM 78 O TYR A 48 14.081 71.520 20.639 1.00 28.34 A O ATOM 79 N LEU A 49 12.138 71.779 21.731 1.00 31.10 A N ATOM 80 CA LEU A 49 12.200 73.232 21.725 1.00 31.20 A C ATOM 81 CB LEU A 49 10.971 73.829 22.416 1.00 29.56 A C ATOM 82 CG LEU A 49 9.648 73.749 21.650 1.00 28.86 A C ATOM 83 CD1 LEU A 49 8.503 74.210 22.530 1.00 29.67 A C ATOM 84 CD2 LEU A 49 9.719 74.588 20.347 1.00 25.11 A C ATOM 85 C LEU A 49 13.470 73.729 22.402 1.00 31.73 A C ATOM 86 O LEU A 49 14.099 74.696 21.963 1.00 30.36 A O ATOM 87 N TYR A 50 13.859 73.084 23.489 1.00 31.65 A N ATOM 88 CA TYR A 50 15.044 73.569 24.176 1.00 33.14 A C ATOM 89 CB TYR A 50 15.209 72.951 25.560 1.00 33.85 A C ATOM 90 CG TYR A 50 16.620 73.091 26.083 1.00 36.42 A C ATOM 91 CD1 TYR A 50 17.047 74.270 26.682 1.00 35.52 A C ATOM 92 CE1 TYR A 50 18.335 74.400 27.157 1.00 39.57 A C ATOM 93 CD2 TYR A 50 17.532 72.046 25.954 1.00 39.41 A C ATOM 94 CE2 TYR A 50 18.829 72.170 26.422 1.00 38.19 A C ATOM 95 CZ TYR A 50 19.221 73.344 27.025 1.00 40.79 A C ATOM 96 OH TYR A 50 20.512 73.459 27.488 1.00 50.96 A O ATOM 97 C TYR A 50 16.274 73.281 23.350 1.00 29.04 A C ATOM 98 O TYR A 50 17.092 74.159 23.120 1.00 30.30 A O ATOM 99 N ARG A 51 16.398 72.044 22.901 1.00 26.80 A N ATOM 100 CA ARG A 51 17.667 71.600 22.382 1.00 30.40 A C ATOM 101 CB ARG A 51 17.802 70.075 22.423 1.00 30.79 A C ATOM 102 CG ARG A 51 17.211 69.310 21.277 1.00 35.26 A C ATOM 103 CD ARG A 51 17.685 67.856 21.352 1.00 33.78 A C ATOM 104 NE ARG A 51 19.137 67.790 21.257 1.00 44.43 A N ATOM 105 CZ ARG A 51 19.899 66.819 21.768 1.00 47.46 A C ATOM 106 NH1 ARG A 51 21.215 66.875 21.614 1.00 41.83 A N ATOM 107 NH2 ARG A 51 19.357 65.802 22.430 1.00 43.17 A N ATOM 108 C ARG A 51 17.975 72.221 21.014 1.00 28.63 A C ATOM 109 O ARG A 51 19.120 72.465 20.709 1.00 27.12 A O ATOM 110 N TYR A 52 16.950 72.571 20.247 1.00 27.07 A N ATOM 111 CA TYR A 52 17.187 73.157 18.938 1.00 28.88 A C ATOM 112 CB TYR A 52 16.267 72.532 17.909 1.00 26.56 A C ATOM 113 CG TYR A 52 16.568 71.059 17.757 1.00 29.11 A C ATOM 114 CD1 TYR A 52 15.627 70.096 18.088 1.00 28.57 A C ATOM 115 CE1 TYR A 52 15.919 68.742 17.953 1.00 33.11 A C ATOM 116 CD2 TYR A 52 17.811 70.637 17.311 1.00 28.47 A C ATOM 117 CE2 TYR A 52 18.115 69.297 17.169 1.00 30.55 A C ATOM 118 CZ TYR A 52 17.168 68.349 17.487 1.00 32.61 A C ATOM 119 OH TYR A 52 17.471 67.006 17.350 1.00 28.55 A O ATOM 120 C TYR A 52 17.142 74.676 18.946 1.00 30.95 A C ATOM 121 O TYR A 52 17.193 75.317 17.897 1.00 25.11 A O ATOM 122 N GLY A 53 17.088 75.250 20.150 1.00 30.29 A N ATOM 123 CA GLY A 53 17.310 76.677 20.324 1.00 29.26 A C ATOM 124 C GLY A 53 16.077 77.544 20.419 1.00 29.30 A C ATOM 125 O GLY A 53 16.169 78.735 20.694 1.00 31.01 A O ATOM 126 N TYR A 54 14.910 76.953 20.203 1.00 32.20 A N ATOM 127 CA TYR A 54 13.661 77.715 20.192 1.00 29.18 A C ATOM 128 CB TYR A 54 12.528 76.831 19.684 1.00 27.83 A C ATOM 129 CG TYR A 54 12.766 76.344 18.280 1.00 31.53 A C ATOM 130 CD1 TYR A 54 13.174 75.038 18.025 1.00 30.02 A C ATOM 131 CE1 TYR A 54 13.399 74.604 16.735 1.00 25.91 A C ATOM 132 CD2 TYR A 54 12.632 77.211 17.206 1.00 29.66 A C ATOM 133 CE2 TYR A 54 12.843 76.790 15.926 1.00 26.68 A C ATOM 134 CZ TYR A 54 13.224 75.493 15.688 1.00 28.65 A C ATOM 135 OH TYR A 54 13.454 75.105 14.378 1.00 29.53 A O ATOM 136 C TYR A 54 13.275 78.356 21.537 1.00 31.81 A C ATOM 137 O TYR A 54 12.699 79.443 21.575 1.00 27.67 A O ATOM 138 N THR A 55 13.588 77.687 22.637 1.00 32.54 A N ATOM 139 CA THR A 55 13.233 78.222 23.947 1.00 33.59 A C ATOM 140 CB THR A 55 13.273 77.132 25.032 1.00 33.04 A C ATOM 141 OG1 THR A 55 14.594 76.574 25.111 1.00 36.18 A O ATOM 142 CG2 THR A 55 12.316 76.038 24.671 1.00 28.50 A C ATOM 143 C THR A 55 14.107 79.423 24.329 1.00 36.78 A C ATOM 144 O THR A 55 13.592 80.444 24.785 1.00 38.31 A O ATOM 145 N ARG A 56 15.418 79.311 24.125 1.00 37.42 A N ATOM 146 CA ARG A 56 16.327 80.440 24.352 1.00 41.03 A C ATOM 147 CB ARG A 56 17.752 80.070 23.911 1.00 39.63 A C ATOM 148 CG ARG A 56 18.786 81.186 24.096 1.00 44.33 A C ATOM 149 CD ARG A 56 19.274 81.321 25.543 1.00 47.51 A C ATOM 150 NE ARG A 56 18.326 82.029 26.399 1.00 44.01 A N ATOM 151 CZ ARG A 56 18.506 83.245 26.914 1.00 44.93 A C ATOM 152 NH1 ARG A 56 19.615 83.936 26.682 1.00 46.99 A N ATOM 153 NH2 ARG A 56 17.561 83.774 27.678 1.00 46.03 A N ATOM 154 C ARG A 56 15.860 81.718 23.632 1.00 38.69 A C ATOM 155 O ARG A 56 15.846 82.807 24.207 1.00 36.67 A O ATOM 156 N VAL A 57 15.484 81.576 22.366 1.00 34.77 A N ATOM 157 CA VAL A 57 14.980 82.700 21.584 1.00 36.17 A C ATOM 158 CB VAL A 57 14.767 82.321 20.108 1.00 37.68 A C ATOM 159 CG1 VAL A 57 14.180 83.496 19.340 1.00 37.21 A C ATOM 160 CG2 VAL A 57 16.085 81.862 19.476 1.00 33.46 A C ATOM 161 C VAL A 57 13.668 83.210 22.163 1.00 35.68 A C ATOM 162 O VAL A 57 13.425 84.417 22.209 1.00 35.23 A O ATOM 163 N GLY A 58 12.823 82.283 22.604 1.00 36.01 A N ATOM 164 CA GLY A 58 11.559 82.628 23.238 1.00 37.49 A C ATOM 165 C GLY A 58 11.785 83.511 24.451 1.00 36.51 A C ATOM 166 O GLY A 58 11.165 84.558 24.597 1.00 39.55 A O ATOM 167 N GLU A 59 12.693 83.086 25.321 1.00 38.00 A N ATOM 168 CA GLU A 59 13.039 83.864 26.509 1.00 41.42 A C ATOM 169 C GLU A 59 13.515 85.272 26.153 1.00 44.35 A C ATOM 170 CB GLU A 59 14.117 83.153 27.318 1.00 38.70 A C ATOM 171 CG GLU A 59 13.795 81.701 27.616 1.00 41.48 A C ATOM 172 CD GLU A 59 14.887 81.018 28.402 1.00 44.95 A C ATOM 173 OE1 GLU A 59 15.975 81.615 28.550 1.00 47.60 A O ATOM 174 OE2 GLU A 59 14.664 79.882 28.871 1.00 48.93 A O ATOM 175 O GLU A 59 13.129 86.245 26.809 1.00 44.06 A O ATOM 176 N MET A 60 14.344 85.375 25.111 1.00 40.89 A N ATOM 177 CA MET A 60 14.900 86.661 24.689 1.00 41.38 A C ATOM 178 C MET A 60 13.817 87.619 24.232 1.00 40.47 A C ATOM 179 CB MET A 60 15.904 86.488 23.547 1.00 39.66 A C ATOM 180 CG MET A 60 17.153 85.711 23.897 1.00 40.81 A C ATOM 181 SD MET A 60 18.251 85.659 22.464 1.00 47.39 A S ATOM 182 CE MET A 60 19.367 84.356 22.960 1.00 44.47 A C ATOM 183 O MET A 60 14.093 88.773 23.927 1.00 41.88 A O ATOM 184 N ARG A 61 12.584 87.134 24.161 1.00 43.73 A N ATOM 185 CA ARG A 61 11.482 87.979 23.725 1.00 40.85 A C ATOM 186 C ARG A 61 10.445 88.115 24.822 1.00 42.71 A C ATOM 187 CB ARG A 61 10.843 87.411 22.466 1.00 41.23 A C ATOM 188 CG ARG A 61 11.835 87.120 21.353 1.00 45.78 A C ATOM 189 CD ARG A 61 11.107 86.814 20.069 1.00 47.99 A C ATOM 190 NE ARG A 61 12.029 86.518 18.982 1.00 50.65 A N ATOM 191 CZ ARG A 61 11.641 86.262 17.737 1.00 50.08 A C ATOM 192 NH1 ARG A 61 12.543 85.997 16.800 1.00 43.93 A N ATOM 193 NH2 ARG A 61 10.346 86.271 17.434 1.00 49.73 A N ATOM 194 O ARG A 61 9.344 88.609 24.580 1.00 45.46 A O ATOM 195 N GLY A 62 10.811 87.670 26.023 1.00 43.12 A N ATOM 196 CA GLY A 62 9.930 87.728 27.179 1.00 45.32 A C ATOM 197 C GLY A 62 8.688 86.874 26.991 1.00 51.72 A C ATOM 198 O GLY A 62 7.646 87.122 27.605 1.00 50.28 A O ATOM 199 N GLU A 63 8.814 85.875 26.118 1.00 49.86 A N ATOM 200 CA GLU A 63 7.759 84.908 25.845 1.00 51.51 A C ATOM 201 C GLU A 63 8.138 83.596 26.499 1.00 55.34 A C ATOM 202 CB GLU A 63 7.587 84.720 24.343 1.00 48.53 A C ATOM 203 CG GLU A 63 6.756 85.811 23.703 1.00 53.52 A C ATOM 204 CD GLU A 63 7.112 86.044 22.246 1.00 55.28 A C ATOM 205 OE1 GLU A 63 6.431 86.861 21.592 1.00 59.70 A O ATOM 206 OE2 GLU A 63 8.077 85.418 21.758 1.00 55.92 A O ATOM 207 O GLU A 63 8.150 82.539 25.864 1.00 53.90 A O ATOM 208 N SER A 64 8.420 83.687 27.794 1.00 59.35 A N ATOM 209 CA SER A 64 9.177 82.663 28.507 1.00 58.38 A C ATOM 210 C SER A 64 8.725 81.204 28.339 1.00 62.15 A C ATOM 211 CB SER A 64 9.429 83.080 29.957 1.00 62.69 A C ATOM 212 OG SER A 64 10.134 84.317 29.963 1.00 59.30 A O ATOM 213 O SER A 64 9.396 80.488 27.592 1.00 64.10 A O ATOM 214 N LYS A 65 7.638 80.718 28.955 1.00 61.32 A N ATOM 215 CA LYS A 65 6.639 81.397 29.789 1.00 58.69 A C ATOM 216 C LYS A 65 5.391 80.522 29.670 1.00 60.03 A C ATOM 217 CB LYS A 65 6.298 82.794 29.276 1.00 59.62 A C ATOM 218 CG LYS A 65 4.832 82.982 28.943 1.00 57.57 A C ATOM 219 CD LYS A 65 4.584 82.994 27.448 1.00 52.86 A C ATOM 220 CE LYS A 65 4.844 84.375 26.887 1.00 49.44 A C ATOM 221 NZ LYS A 65 3.838 84.764 25.860 1.00 54.03 A N ATOM 222 O LYS A 65 4.399 80.702 30.379 1.00 67.06 A O ATOM 223 N SER A 66 5.496 79.542 28.779 1.00 58.28 A N ATOM 224 CA SER A 66 4.384 78.819 28.176 1.00 52.97 A C ATOM 225 C SER A 66 4.978 78.372 26.843 1.00 50.97 A C ATOM 226 CB SER A 66 3.191 79.749 27.937 1.00 49.09 A C ATOM 227 OG SER A 66 2.503 79.421 26.735 1.00 49.00 A O ATOM 228 O SER A 66 5.879 79.031 26.332 1.00 48.04 A O ATOM 229 N LEU A 67 4.507 77.269 26.276 1.00 45.40 A N ATOM 230 CA LEU A 67 5.136 76.754 25.058 1.00 44.93 A C ATOM 231 C LEU A 67 4.783 77.547 23.799 1.00 41.46 A C ATOM 232 CB LEU A 67 4.786 75.278 24.845 1.00 45.20 A C ATOM 233 CG LEU A 67 5.407 74.265 25.799 1.00 42.42 A C ATOM 234 CD1 LEU A 67 5.026 72.861 25.393 1.00 47.76 A C ATOM 235 CD2 LEU A 67 6.900 74.406 25.819 1.00 44.45 A C ATOM 236 O LEU A 67 5.545 77.569 22.822 1.00 37.58 A O ATOM 237 N GLY A 68 3.622 78.185 23.825 1.00 39.26 A N ATOM 238 CA GLY A 68 3.069 78.831 22.651 1.00 39.10 A C ATOM 239 C GLY A 68 4.079 79.519 21.758 1.00 36.77 A C ATOM 240 O GLY A 68 4.268 79.129 20.611 1.00 39.15 A O ATOM 241 N PRO A 69 4.728 80.564 22.275 1.00 39.44 A N ATOM 242 CD PRO A 69 4.557 81.151 23.615 1.00 43.10 A C ATOM 243 CA PRO A 69 5.676 81.326 21.461 1.00 38.28 A C ATOM 244 CB PRO A 69 6.228 82.356 22.446 1.00 43.32 A C ATOM 245 CG PRO A 69 5.107 82.539 23.433 1.00 46.06 A C ATOM 246 C PRO A 69 6.785 80.454 20.871 1.00 35.43 A C ATOM 247 O PRO A 69 7.047 80.596 19.671 1.00 33.15 A O ATOM 248 N ALA A 70 7.397 79.572 21.664 1.00 32.48 A N ATOM 249 CA ALA A 70 8.448 78.680 21.152 1.00 34.98 A C ATOM 250 CB ALA A 70 9.023 77.802 22.274 1.00 28.82 A C ATOM 251 C ALA A 70 7.969 77.800 19.987 1.00 36.25 A C ATOM 252 O ALA A 70 8.706 77.591 19.008 1.00 33.30 A O ATOM 253 N LEU A 71 6.747 77.275 20.111 1.00 31.36 A N ATOM 254 CA LEU A 71 6.152 76.430 19.079 1.00 29.55 A C ATOM 255 CB LEU A 71 4.789 75.894 19.534 1.00 32.08 A C ATOM 256 CG LEU A 71 4.755 74.870 20.669 1.00 32.54 A C ATOM 257 CD1 LEU A 71 3.325 74.701 21.217 1.00 33.32 A C ATOM 258 CD2 LEU A 71 5.322 73.533 20.212 1.00 29.69 A C ATOM 259 C LEU A 71 5.970 77.220 17.795 1.00 32.24 A C ATOM 260 O LEU A 71 6.119 76.694 16.685 1.00 32.92 A O ATOM 261 N LEU A 72 5.627 78.489 17.951 1.00 33.75 A N ATOM 262 CA LEU A 72 5.405 79.349 16.806 1.00 32.89 A C ATOM 263 CB LEU A 72 4.852 80.697 17.265 1.00 33.96 A C ATOM 264 CG LEU A 72 4.169 81.585 16.228 1.00 39.41 A C ATOM 265 CD1 LEU A 72 3.125 80.814 15.447 1.00 40.95 A C ATOM 266 CD2 LEU A 72 3.539 82.792 16.914 1.00 44.13 A C ATOM 267 C LEU A 72 6.712 79.534 16.037 1.00 33.92 A C ATOM 268 O LEU A 72 6.747 79.385 14.815 1.00 32.15 A O ATOM 269 N LEU A 73 7.783 79.852 16.758 1.00 33.84 A N ATOM 270 CA LEU A 73 9.095 80.031 16.133 1.00 34.27 A C ATOM 271 CB LEU A 73 10.140 80.452 17.169 1.00 34.92 A C ATOM 272 CG LEU A 73 9.933 81.785 17.889 1.00 39.25 A C ATOM 273 CD1 LEU A 73 10.997 81.984 18.962 1.00 35.24 A C ATOM 274 CD2 LEU A 73 9.937 82.937 16.889 1.00 38.29 A C ATOM 275 C LEU A 73 9.548 78.745 15.446 1.00 33.43 A C ATOM 276 O LEU A 73 10.207 78.787 14.397 1.00 32.04 A O ATOM 277 N LEU A 74 9.209 77.603 16.045 1.00 29.42 A N ATOM 278 CA LEU A 74 9.584 76.317 15.476 1.00 30.39 A C ATOM 279 CB LEU A 74 9.325 75.178 16.467 1.00 28.90 A C ATOM 280 CG LEU A 74 9.415 73.715 16.014 1.00 29.89 A C ATOM 281 CD1 LEU A 74 9.585 72.775 17.217 1.00 29.86 A C ATOM 282 CD2 LEU A 74 8.193 73.295 15.217 1.00 27.65 A C ATOM 283 C LEU A 74 8.836 76.085 14.166 1.00 32.43 A C ATOM 284 O LEU A 74 9.418 75.622 13.184 1.00 28.46 A O ATOM 285 N GLN A 75 7.551 76.422 14.172 1.00 29.84 A N ATOM 286 CA GLN A 75 6.680 76.259 13.019 1.00 29.56 A C ATOM 287 CB GLN A 75 5.233 76.544 13.416 1.00 31.35 A C ATOM 288 CG GLN A 75 4.582 75.367 14.113 1.00 31.39 A C ATOM 289 CD GLN A 75 3.481 75.770 15.077 1.00 33.36 A C ATOM 290 OE1 GLN A 75 3.065 76.930 15.131 1.00 34.75 A O ATOM 291 NE2 GLN A 75 2.982 74.801 15.823 1.00 28.27 A N ATOM 292 C GLN A 75 7.103 77.154 11.855 1.00 32.66 A C ATOM 293 O GLN A 75 7.003 76.768 10.681 1.00 29.20 A O ATOM 294 N LYS A 76 7.567 78.351 12.192 1.00 30.39 A N ATOM 295 CA LYS A 76 8.144 79.246 11.203 1.00 33.96 A C ATOM 296 CB LYS A 76 8.403 80.625 11.802 1.00 30.20 A C ATOM 297 CG LYS A 76 7.238 81.587 11.629 1.00 42.11 A C ATOM 298 CD LYS A 76 7.134 82.548 12.810 1.00 40.94 A C ATOM 299 CE LYS A 76 5.885 83.411 12.725 1.00 46.18 A C ATOM 300 NZ LYS A 76 5.840 84.366 13.878 1.00 57.58 A N ATOM 301 C LYS A 76 9.441 78.684 10.649 1.00 32.56 A C ATOM 302 O LYS A 76 9.651 78.682 9.442 1.00 30.30 A O ATOM 303 N GLN A 77 10.309 78.212 11.538 1.00 30.55 A N ATOM 304 CA GLN A 77 11.631 77.748 11.130 1.00 29.82 A C ATOM 305 CB GLN A 77 12.537 77.527 12.348 1.00 31.37 A C ATOM 306 CG GLN A 77 13.951 77.036 12.014 1.00 34.58 A C ATOM 307 CD GLN A 77 14.791 78.060 11.262 1.00 37.61 A C ATOM 308 OE1 GLN A 77 14.567 79.267 11.371 1.00 37.52 A O ATOM 309 NE2 GLN A 77 15.766 77.572 10.484 1.00 37.26 A N ATOM 310 C GLN A 77 11.559 76.488 10.282 1.00 32.47 A C ATOM 311 O GLN A 77 12.439 76.240 9.447 1.00 34.40 A O ATOM 312 N LEU A 78 10.503 75.709 10.458 1.00 28.33 A N ATOM 313 CA LEU A 78 10.406 74.429 9.772 1.00 28.74 A C ATOM 314 CB LEU A 78 10.133 73.301 10.759 1.00 27.70 A C ATOM 315 CG LEU A 78 11.123 73.108 11.899 1.00 31.78 A C ATOM 316 CD1 LEU A 78 10.697 71.913 12.725 1.00 31.16 A C ATOM 317 CD2 LEU A 78 12.494 72.895 11.335 1.00 31.42 A C ATOM 318 C LEU A 78 9.332 74.423 8.717 1.00 27.24 A C ATOM 319 O LEU A 78 9.042 73.376 8.141 1.00 28.52 A O ATOM 320 N SER A 79 8.729 75.588 8.479 1.00 30.48 A N ATOM 321 CA SER A 79 7.648 75.717 7.498 1.00 28.97 A C ATOM 322 CB SER A 79 8.182 75.493 6.084 1.00 28.47 A C ATOM 323 OG SER A 79 9.172 76.468 5.815 1.00 30.36 A O ATOM 324 C SER A 79 6.450 74.812 7.771 1.00 31.91 A C ATOM 325 O SER A 79 5.879 74.227 6.854 1.00 32.10 A O ATOM 326 N LEU A 80 6.072 74.705 9.036 1.00 30.77 A N ATOM 327 CA LEU A 80 4.817 74.069 9.400 1.00 31.64 A C ATOM 328 CB LEU A 80 4.956 73.322 10.726 1.00 31.22 A C ATOM 329 CG LEU A 80 6.231 72.500 10.921 1.00 33.12 A C ATOM 330 CD1 LEU A 80 6.333 72.011 12.366 1.00 28.23 A C ATOM 331 CD2 LEU A 80 6.258 71.337 9.958 1.00 30.41 A C ATOM 332 C LEU A 80 3.773 75.170 9.546 1.00 33.72 A C ATOM 333 O LEU A 80 4.124 76.345 9.608 1.00 37.46 A O ATOM 334 N PRO A 81 2.486 74.799 9.601 1.00 35.06 A N ATOM 335 CD PRO A 81 1.919 73.469 9.323 1.00 33.78 A C ATOM 336 CA PRO A 81 1.445 75.801 9.875 1.00 35.72 A C ATOM 337 CB PRO A 81 0.156 74.976 9.858 1.00 36.70 A C ATOM 338 CG PRO A 81 0.488 73.774 9.015 1.00 36.26 A C ATOM 339 C PRO A 81 1.644 76.494 11.232 1.00 34.20 A C ATOM 340 O PRO A 81 1.879 75.848 12.259 1.00 33.23 A O ATOM 341 N GLU A 82 1.542 77.816 11.218 1.00 34.37 A N ATOM 342 CA GLU A 82 1.895 78.637 12.372 1.00 35.46 A C ATOM 343 CB GLU A 82 2.529 79.941 11.890 1.00 35.12 A C ATOM 344 CG GLU A 82 3.652 79.643 10.894 1.00 36.40 A C ATOM 345 CD GLU A 82 4.218 80.861 10.214 1.00 43.11 A C ATOM 346 OE1 GLU A 82 3.978 81.991 10.690 1.00 44.74 A O ATOM 347 OE2 GLU A 82 4.922 80.678 9.192 1.00 44.33 A O ATOM 348 C GLU A 82 0.702 78.844 13.314 1.00 39.51 A C ATOM 349 O GLU A 82 0.070 79.905 13.361 1.00 39.72 A O ATOM 350 N THR A 83 0.407 77.784 14.056 1.00 36.38 A N ATOM 351 CA THR A 83 −0.734 77.736 14.953 1.00 37.67 A C ATOM 352 CB THR A 83 −1.317 76.333 14.944 1.00 36.43 A C ATOM 353 OG1 THR A 83 −0.360 75.419 15.502 1.00 32.72 A O ATOM 354 CG2 THR A 83 −1.625 75.915 13.510 1.00 31.41 A C ATOM 355 C THR A 83 −0.291 78.064 16.375 1.00 37.84 A C ATOM 356 O THR A 83 −1.104 78.405 17.230 1.00 36.20 A O ATOM 357 N GLY A 84 1.012 77.970 16.620 1.00 36.65 A N ATOM 358 CA GLY A 84 1.525 78.166 17.961 1.00 36.39 A C ATOM 359 C GLY A 84 0.904 77.158 18.913 1.00 36.79 A C ATOM 360 O GLY A 84 0.801 77.406 20.119 1.00 37.31 A O ATOM 361 N GLU A 85 0.491 76.014 18.372 1.00 33.76 A N ATOM 362 CA GLU A 85 −0.085 74.950 19.192 1.00 36.02 A C ATOM 363 CB GLU A 85 −1.542 74.657 18.783 1.00 30.97 A C ATOM 364 CG GLU A 85 −2.517 75.831 18.922 1.00 31.51 A C ATOM 365 CD GLU A 85 −2.953 76.094 20.377 1.00 35.89 A C ATOM 366 OE1 GLU A 85 −2.576 75.323 21.298 1.00 32.12 A O ATOM 367 OE2 GLU A 85 −3.691 77.078 20.596 1.00 38.22 A O ATOM 368 C GLU A 85 0.751 73.689 19.031 1.00 33.43 A C ATOM 369 O GLU A 85 1.283 73.428 17.948 1.00 33.17 A O ATOM 370 N LEU A 86 0.874 72.921 20.108 1.00 33.30 A N ATOM 371 CA LEU A 86 1.427 71.582 20.038 1.00 33.20 A C ATOM 372 CB LEU A 86 1.741 71.044 21.441 1.00 28.84 A C ATOM 373 CG LEU A 86 2.373 69.652 21.517 1.00 31.21 A C ATOM 374 CD1 LEU A 86 3.522 69.515 20.516 1.00 33.17 A C ATOM 375 CD2 LEU A 86 2.876 69.357 22.915 1.00 34.51 A C ATOM 376 C LEU A 86 0.380 70.720 19.348 1.00 32.87 A C ATOM 377 O LEU A 86 −0.309 69.928 19.994 1.00 34.20 A O ATOM 378 N ASP A 87 0.252 70.893 18.035 1.00 30.27 A N ATOM 379 CA ASP A 87 −0.764 70.188 17.252 1.00 30.67 A C ATOM 380 CB ASP A 87 −1.367 71.127 16.208 1.00 29.91 A C ATOM 381 CG ASP A 87 −0.307 71.765 15.320 1.00 31.84 A C ATOM 382 OD1 ASP A 87 0.770 71.152 15.167 1.00 31.10 A O ATOM 383 OD2 ASP A 87 −0.561 72.867 14.776 1.00 31.61 A O ATOM 384 C ASP A 87 −0.187 68.938 16.582 1.00 33.08 A C ATOM 385 O ASP A 87 0.957 68.556 16.846 1.00 27.45 A O ATOM 386 N SER A 88 −0.979 68.307 15.719 1.00 31.20 A N ATOM 387 CA SER A 88 −0.571 67.043 15.110 1.00 31.46 A C ATOM 388 CB SER A 88 −1.739 66.387 14.354 1.00 30.83 A C ATOM 389 OG SER A 88 −2.733 65.904 15.253 1.00 39.76 A O ATOM 390 C SER A 88 0.654 67.193 14.198 1.00 28.33 A C ATOM 391 O SER A 88 1.568 66.367 14.241 1.00 29.84 A O ATOM 392 N ALA A 89 0.665 68.225 13.361 1.00 29.74 A N ATOM 393 CA ALA A 89 1.796 68.416 12.449 1.00 30.30 A C ATOM 394 CB ALA A 89 1.570 69.583 11.526 1.00 28.19 A C ATOM 395 C ALA A 89 3.061 68.620 13.266 1.00 30.62 A C ATOM 396 O ALA A 89 4.087 68.002 12.990 1.00 29.25 A O ATOM 397 N THR A 90 2.975 69.464 14.293 1.00 28.12 A N ATOM 398 CA THR A 90 4.161 69.808 15.080 1.00 27.36 A C ATOM 399 CB THR A 90 3.911 71.007 15.992 1.00 28.15 A C ATOM 400 OG1 THR A 90 3.536 72.133 15.194 1.00 28.03 A O ATOM 401 CG2 THR A 90 5.153 71.344 16.783 1.00 25.06 A C ATOM 402 C THR A 90 4.714 68.619 15.856 1.00 28.43 A C ATOM 403 O THR A 90 5.925 68.418 15.901 1.00 29.06 A O ATOM 404 N LEU A 91 3.836 67.812 16.436 1.00 25.19 A N ATOM 405 CA LEU A 91 4.272 66.601 17.124 1.00 25.70 A C ATOM 406 CB LEU A 91 3.077 65.891 17.735 1.00 31.92 A C ATOM 407 CG LEU A 91 3.434 64.819 18.763 1.00 36.55 A C ATOM 408 CD1 LEU A 91 4.507 65.346 19.698 1.00 37.27 A C ATOM 409 CD2 LEU A 91 2.190 64.394 19.553 1.00 36.39 A C ATOM 410 C LEU A 91 4.976 65.638 16.174 1.00 29.70 A C ATOM 411 O LEU A 91 6.021 65.062 16.493 1.00 29.11 A O ATOM 412 N LYS A 92 4.385 65.455 15.003 1.00 29.12 A N ATOM 413 CA LYS A 92 4.922 64.527 14.041 1.00 32.10 A C ATOM 414 CB LYS A 92 3.978 64.388 12.841 1.00 32.19 A C ATOM 415 CG LYS A 92 4.558 63.538 11.724 1.00 39.19 A C ATOM 416 CD LYS A 92 3.754 63.656 10.437 1.00 47.21 A C ATOM 417 CE LYS A 92 4.629 63.327 9.219 1.00 48.85 A C ATOM 418 NZ LYS A 92 3.892 63.445 7.927 1.00 52.75 A N ATOM 419 C LYS A 92 6.294 65.063 13.622 1.00 31.23 A C ATOM 420 O LYS A 92 7.284 64.325 13.620 1.00 28.50 A O ATOM 421 N ALA A 93 6.345 66.355 13.305 1.00 25.66 A N ATOM 422 CA ALA A 93 7.612 67.004 13.007 1.00 29.53 A C ATOM 423 CB ALA A 93 7.451 68.516 12.884 1.00 26.65 A C ATOM 424 C ALA A 93 8.632 66.668 14.084 1.00 30.38 A C ATOM 425 O ALA A 93 9.711 66.185 13.771 1.00 28.12 A O ATOM 426 N MET A 94 8.281 66.906 15.349 1.00 28.01 A N ATOM 427 CA MET A 94 9.195 66.659 16.462 1.00 28.21 A C ATOM 428 CB MET A 94 8.563 67.080 17.796 1.00 29.43 A C ATOM 429 CG MET A 94 8.398 68.573 17.961 1.00 30.64 A C ATOM 430 SD MET A 94 7.441 68.988 19.432 1.00 29.03 A S ATOM 431 CE MET A 94 7.484 70.776 19.418 1.00 26.52 A C ATOM 432 C MET A 94 9.642 65.205 16.575 1.00 29.47 A C ATOM 433 O MET A 94 10.722 64.922 17.095 1.00 32.13 A O ATOM 434 N ARG A 95 8.801 64.284 16.119 1.00 28.08 A N ATOM 435 CA ARG A 95 9.120 62.860 16.178 1.00 27.32 A C ATOM 436 CB ARG A 95 7.841 62.018 16.199 1.00 32.95 A C ATOM 437 CG ARG A 95 7.044 61.981 17.510 1.00 36.73 A C ATOM 438 CD ARG A 95 6.136 60.741 17.470 1.00 37.06 A C ATOM 439 NE ARG A 95 4.949 60.838 18.310 1.00 50.40 A N ATOM 440 CZ ARG A 95 3.719 61.079 17.855 1.00 49.89 A C ATOM 441 NH1 ARG A 95 3.500 61.265 16.551 1.00 43.80 A N ATOM 442 NH2 ARG A 95 2.702 61.143 18.710 1.00 48.67 A N ATOM 443 C ARG A 95 9.970 62.399 14.981 1.00 29.53 A C ATOM 444 O ARG A 95 10.374 61.245 14.913 1.00 30.39 A O ATOM 445 N THR A 96 10.218 63.292 14.032 1.00 27.31 A N ATOM 446 CA THR A 96 10.961 62.927 12.827 1.00 31.53 A C ATOM 447 CB THR A 96 10.574 63.843 11.649 1.00 28.90 A C ATOM 448 OG1 THR A 96 9.153 63.793 11.459 1.00 30.87 A O ATOM 449 CG2 THR A 96 11.258 63.401 10.355 1.00 29.04 A C ATOM 450 C THR A 96 12.476 62.954 13.094 1.00 26.66 A C ATOM 451 O THR A 96 12.989 63.919 13.671 1.00 25.71 A O ATOM 452 N PRO A 97 13.189 61.878 12.706 1.00 28.60 A N ATOM 453 CD PRO A 97 12.683 60.671 12.030 1.00 31.95 A C ATOM 454 CA PRO A 97 14.652 61.843 12.859 1.00 30.12 A C ATOM 455 CB PRO A 97 15.053 60.532 12.176 1.00 29.20 A C ATOM 456 CG PRO A 97 13.813 59.699 12.198 1.00 33.13 A C ATOM 457 C PRO A 97 15.260 63.030 12.123 1.00 29.08 A C ATOM 458 O PRO A 97 14.713 63.439 11.109 1.00 31.50 A O ATOM 459 N ARG A 98 16.345 63.593 12.638 1.00 29.10 A N ATOM 460 CA ARG A 98 16.869 64.842 12.097 1.00 26.45 A C ATOM 461 CB ARG A 98 16.047 66.037 12.577 1.00 28.80 A C ATOM 462 CG ARG A 98 15.940 66.148 14.131 1.00 26.39 A C ATOM 463 CD ARG A 98 15.555 67.566 14.549 1.00 25.63 A C ATOM 464 NE ARG A 98 16.675 68.475 14.350 1.00 30.70 A N ATOM 465 CZ ARG A 98 16.568 69.785 14.147 1.00 27.35 A C ATOM 466 NH1 ARG A 98 15.379 70.362 14.111 1.00 27.88 A N ATOM 467 NH2 ARG A 98 17.662 70.513 13.966 1.00 24.71 A N ATOM 468 C ARG A 98 18.299 65.043 12.525 1.00 28.07 A C ATOM 469 O ARG A 98 18.835 64.257 13.300 1.00 27.23 A O ATOM 470 N CYS A 99 18.901 66.103 11.993 1.00 25.30 A N ATOM 471 CA CYS A 99 20.228 66.549 12.377 1.00 28.60 A C ATOM 472 CB CYS A 99 20.669 67.637 11.413 1.00 23.56 A C ATOM 473 SG CYS A 99 22.289 68.278 11.777 1.00 26.28 A S ATOM 474 C CYS A 99 20.276 67.127 13.790 1.00 25.38 A C ATOM 475 O CYS A 99 19.424 67.919 14.164 1.00 25.26 A O ATOM 476 N GLY A 100 21.311 66.783 14.544 1.00 28.00 A N ATOM 477 CA GLY A 100 21.456 67.261 15.910 1.00 27.71 A C ATOM 478 C GLY A 100 21.923 68.707 16.061 1.00 30.00 A C ATOM 479 O GLY A 100 21.973 69.242 17.166 1.00 25.78 A O ATOM 480 N VAL A 101 22.276 69.350 14.953 1.00 29.21 A N ATOM 481 CA VAL A 101 22.718 70.742 15.002 1.00 27.22 A C ATOM 482 CB VAL A 101 23.420 71.158 13.666 1.00 27.17 A C ATOM 483 CG1 VAL A 101 23.603 72.680 13.569 1.00 28.66 A C ATOM 484 CG2 VAL A 101 24.758 70.467 13.545 1.00 24.07 A C ATOM 485 C VAL A 101 21.494 71.614 15.290 1.00 27.29 A C ATOM 486 O VAL A 101 20.433 71.382 14.728 1.00 28.30 A O ATOM 487 N PRO A 102 21.637 72.614 16.170 1.00 27.10 A N ATOM 488 CD PRO A 102 22.833 72.839 16.999 1.00 32.08 A C ATOM 489 CA PRO A 102 20.557 73.553 16.506 1.00 27.20 A C ATOM 490 CB PRO A 102 21.243 74.544 17.444 1.00 30.08 A C ATOM 491 CG PRO A 102 22.338 73.774 18.057 1.00 33.36 A C ATOM 492 C PRO A 102 19.978 74.305 15.313 1.00 28.11 A C ATOM 493 O PRO A 102 20.674 74.538 14.336 1.00 27.56 A O ATOM 494 N ASP A 103 18.714 74.705 15.400 1.00 27.06 A N ATOM 495 CA ASP A 103 18.112 75.469 14.314 1.00 30.43 A C ATOM 496 CB ASP A 103 16.617 75.178 14.206 1.00 28.37 A C ATOM 497 CG ASP A 103 16.335 73.742 13.860 1.00 25.65 A C ATOM 498 OD1 ASP A 103 17.218 73.081 13.286 1.00 26.49 A O ATOM 499 OD2 ASP A 103 15.224 73.269 14.158 1.00 25.92 A O ATOM 500 C ASP A 103 18.321 76.958 14.520 1.00 33.99 A C ATOM 501 O ASP A 103 18.487 77.708 13.555 1.00 27.29 A O ATOM 502 N LEU A 104 18.274 77.380 15.783 1.00 28.21 A N ATOM 503 CA LEU A 104 18.480 78.772 16.136 1.00 28.15 A C ATOM 504 CB LEU A 104 17.216 79.367 16.740 1.00 32.49 A C ATOM 505 CG LEU A 104 16.035 79.514 15.783 1.00 31.16 A C ATOM 506 CD1 LEU A 104 14.777 79.978 16.502 1.00 34.26 A C ATOM 507 CD2 LEU A 104 16.421 80.492 14.700 1.00 35.51 A C ATOM 508 C LEU A 104 19.628 78.847 17.114 1.00 35.40 A C ATOM 509 O LEU A 104 19.638 78.141 18.107 1.00 36.07 A O ATOM 510 N GLY A 105 20.613 79.684 16.814 1.00 44.28 A N ATOM 511 CA GLY A 105 21.810 79.746 17.634 1.00 41.90 A C ATOM 512 C GLY A 105 22.809 78.663 17.270 1.00 46.32 A C ATOM 513 O GLY A 105 22.758 78.068 16.186 1.00 41.38 A O ATOM 514 N ARG A 106 23.733 78.402 18.183 1.00 49.26 A N ATOM 515 CA ARG A 106 24.782 77.428 17.921 1.00 46.50 A C ATOM 516 CB ARG A 106 26.057 78.123 17.432 1.00 47.78 A C ATOM 517 CG ARG A 106 25.825 78.911 16.148 1.00 43.45 A C ATOM 518 CD ARG A 106 27.103 79.156 15.360 1.00 47.73 A C ATOM 519 NE ARG A 106 26.844 79.286 13.920 1.00 45.35 A N ATOM 520 CZ ARG A 106 26.819 78.258 13.074 1.00 42.33 A C ATOM 521 NH1 ARG A 106 27.034 77.023 13.520 1.00 43.35 A N ATOM 522 NH2 ARG A 106 26.588 78.457 11.781 1.00 39.80 A N ATOM 523 C ARG A 106 25.061 76.555 19.140 1.00 49.59 A C ATOM 524 O ARG A 106 24.598 76.843 20.251 1.00 49.49 A O ATOM 525 N PHE A 107 25.786 75.465 18.910 1.00 47.61 A N ATOM 526 CA PHE A 107 26.213 74.591 19.989 1.00 51.46 A C ATOM 527 CB PHE A 107 27.233 73.589 19.462 1.00 46.92 A C ATOM 528 CG PHE A 107 26.629 72.371 18.826 1.00 45.06 A C ATOM 529 CD1 PHE A 107 25.675 71.615 19.503 1.00 40.50 A C ATOM 530 CD2 PHE A 107 27.056 71.956 17.567 1.00 37.67 A C ATOM 531 CE1 PHE A 107 25.130 70.479 18.916 1.00 45.47 A C ATOM 532 CE2 PHE A 107 26.536 70.820 16.981 1.00 36.50 A C ATOM 533 CZ PHE A 107 25.571 70.078 17.644 1.00 38.83 A C ATOM 534 C PHE A 107 26.871 75.407 21.098 1.00 52.66 A C ATOM 535 O PHE A 107 26.525 75.284 22.284 1.00 55.56 A O ATOM 536 N GLN A 108 27.827 76.237 20.686 1.00 49.51 A N ATOM 537 CA GLN A 108 28.694 76.956 21.600 1.00 50.29 A C ATOM 538 CB GLN A 108 29.850 76.043 22.018 1.00 46.60 A C ATOM 539 CG GLN A 108 30.602 75.432 20.850 1.00 48.74 A C ATOM 540 CD GLN A 108 31.737 74.511 21.289 1.00 52.45 A C ATOM 541 OE1 GLN A 108 31.503 73.386 21.734 1.00 52.06 A O ATOM 542 NE2 GLN A 108 32.976 74.984 21.153 1.00 50.59 A N ATOM 543 C GLN A 108 29.221 78.213 20.914 1.00 49.62 A C ATOM 544 O GLN A 108 28.945 78.443 19.736 1.00 48.83 A O ATOM 545 N THR A 109 29.956 79.042 21.645 1.00 45.71 A N ATOM 546 CA THR A 109 30.722 80.089 20.995 1.00 47.87 A C ATOM 547 CB THR A 109 31.276 81.113 21.992 1.00 50.01 A C ATOM 548 OG1 THR A 109 32.101 80.446 22.957 1.00 54.86 A O ATOM 549 CG2 THR A 109 30.139 81.828 22.688 1.00 40.16 A C ATOM 550 C THR A 109 31.884 79.420 20.273 1.00 46.68 A C ATOM 551 O THR A 109 32.538 78.546 20.831 1.00 48.02 A O ATOM 552 N PHE A 110 32.123 79.824 19.029 1.00 44.86 A N ATOM 553 CA PHE A 110 33.150 79.206 18.207 1.00 43.76 A C ATOM 554 CB PHE A 110 32.555 78.668 16.895 1.00 41.70 A C ATOM 555 CG PHE A 110 31.691 77.439 17.060 1.00 40.60 A C ATOM 556 CD1 PHE A 110 30.328 77.498 16.823 1.00 38.17 A C ATOM 557 CD2 PHE A 110 32.249 76.218 17.421 1.00 38.46 A C ATOM 558 CE1 PHE A 110 29.532 76.372 16.957 1.00 37.15 A C ATOM 559 CE2 PHE A 110 31.456 75.090 17.556 1.00 39.40 A C ATOM 560 CZ PHE A 110 30.091 75.172 17.324 1.00 36.84 A C ATOM 561 C PHE A 110 34.263 80.200 17.886 1.00 48.73 A C ATOM 562 O PHE A 110 34.116 81.412 18.074 1.00 48.74 A O ATOM 563 N GLU A 111 35.372 79.677 17.383 1.00 43.32 A N ATOM 564 CA GLU A 111 36.509 80.508 17.043 1.00 45.18 A C ATOM 565 CB GLU A 111 37.799 79.731 17.275 1.00 45.39 A C ATOM 566 CG GLU A 111 38.068 79.433 18.735 1.00 53.73 A C ATOM 567 CD GLU A 111 39.155 80.330 19.302 1.00 61.90 A C ATOM 568 OE1 GLU A 111 38.823 81.338 19.969 1.00 56.57 A O ATOM 569 OE2 GLU A 111 40.347 80.022 19.065 1.00 61.94 A O ATOM 570 C GLU A 111 36.419 80.944 15.595 1.00 45.00 A C ATOM 571 O GLU A 111 36.141 80.126 14.715 1.00 45.53 A O ATOM 572 N GLY A 112 36.644 82.233 15.354 1.00 43.11 A N ATOM 573 CA GLY A 112 36.789 82.741 14.003 1.00 38.83 A C ATOM 574 C GLY A 112 35.523 83.083 13.235 1.00 42.29 A C ATOM 575 O GLY A 112 34.457 83.333 13.801 1.00 36.82 A O ATOM 576 N ASP A 113 35.679 83.037 11.919 1.00 39.15 A N ATOM 577 CA ASP A 113 34.750 83.489 10.899 1.00 38.17 A C ATOM 578 CB ASP A 113 35.556 83.593 9.598 1.00 42.85 A C ATOM 579 CG ASP A 113 35.090 84.705 8.726 1.00 45.55 A C ATOM 580 OD1 ASP A 113 34.243 85.484 9.209 1.00 53.75 A O ATOM 581 OD2 ASP A 113 35.568 84.806 7.576 1.00 44.65 A O ATOM 582 C ASP A 113 33.590 82.532 10.608 1.00 40.89 A C ATOM 583 O ASP A 113 32.511 82.963 10.185 1.00 39.79 A O ATOM 584 N LEU A 114 33.852 81.236 10.777 1.00 37.51 A N ATOM 585 CA LEU A 114 32.932 80.163 10.392 1.00 37.69 A C ATOM 586 CB LEU A 114 31.525 80.398 10.951 1.00 35.57 A C ATOM 587 CG LEU A 114 31.544 80.794 12.432 1.00 42.35 A C ATOM 588 CD1 LEU A 114 30.129 81.018 12.965 1.00 40.76 A C ATOM 589 CD2 LEU A 114 32.308 79.755 13.272 1.00 39.56 A C ATOM 590 C LEU A 114 32.903 79.951 8.877 1.00 39.24 A C ATOM 591 O LEU A 114 31.954 79.383 8.333 1.00 35.36 A O ATOM 592 N LYS A 115 33.962 80.411 8.216 1.00 37.82 A N ATOM 593 CA LYS A 115 34.165 80.249 6.775 1.00 40.02 A C ATOM 594 CB LYS A 115 33.978 81.608 6.081 1.00 42.34 A C ATOM 595 CG LYS A 115 34.372 81.690 4.624 1.00 43.05 A C ATOM 596 CD LYS A 115 34.179 83.112 4.078 1.00 45.97 A C ATOM 597 CE LYS A 115 34.558 83.198 2.598 1.00 51.38 A C ATOM 598 NZ LYS A 115 34.230 84.520 1.963 1.00 56.46 A N ATOM 599 C LYS A 115 35.591 79.739 6.586 1.00 36.72 A C ATOM 600 O LYS A 115 36.484 80.160 7.309 1.00 38.11 A O ATOM 601 N TRP A 116 35.803 78.818 5.649 1.00 34.05 A N ATOM 602 CA TRP A 116 37.165 78.383 5.316 1.00 40.46 A C ATOM 603 CB TRP A 116 37.177 77.114 4.457 1.00 34.45 A C ATOM 604 CG TRP A 116 36.709 75.906 5.160 1.00 37.90 A C ATOM 605 CD2 TRP A 116 37.329 75.276 6.284 1.00 35.52 A C ATOM 606 CE2 TRP A 116 36.535 74.169 6.634 1.00 34.36 A C ATOM 607 CE3 TRP A 116 38.472 75.551 7.039 1.00 38.92 A C ATOM 608 CD1 TRP A 116 35.592 75.170 4.874 1.00 32.16 A C ATOM 609 NE1 TRP A 116 35.490 74.118 5.751 1.00 31.90 A N ATOM 610 CZ2 TRP A 116 36.854 73.326 7.690 1.00 35.38 A C ATOM 611 CZ3 TRP A 116 38.788 74.708 8.096 1.00 37.99 A C ATOM 612 CH2 TRP A 116 37.982 73.617 8.410 1.00 39.00 A C ATOM 613 C TRP A 116 37.897 79.471 4.545 1.00 43.89 A C ATOM 614 O TRP A 116 37.328 80.098 3.645 1.00 44.49 A O ATOM 615 N HIS A 117 39.165 79.675 4.880 1.00 42.33 A N ATOM 616 CA HIS A 117 39.958 80.683 4.206 1.00 40.57 A C ATOM 617 CB HIS A 117 40.439 81.735 5.202 1.00 42.81 A C ATOM 618 CG HIS A 117 39.327 82.542 5.791 1.00 44.04 A C ATOM 619 CD2 HIS A 117 38.735 82.490 7.007 1.00 44.87 A C ATOM 620 ND1 HIS A 117 38.674 83.531 5.088 1.00 43.72 A N ATOM 621 CE1 HIS A 117 37.737 84.064 5.849 1.00 46.67 A C ATOM 622 NE2 HIS A 117 37.748 83.447 7.019 1.00 44.47 A N ATOM 623 C HIS A 117 41.109 80.051 3.434 1.00 39.19 A C ATOM 624 O HIS A 117 42.160 80.660 3.255 1.00 36.97 A O ATOM 625 N HIS A 118 40.895 78.804 3.028 1.00 34.01 A N ATOM 626 CA HIS A 118 41.694 78.151 2.006 1.00 37.93 A C ATOM 627 CB HIS A 118 42.851 77.333 2.592 1.00 36.51 A C ATOM 628 CG HIS A 118 42.440 76.275 3.568 1.00 34.63 A C ATOM 629 CD2 HIS A 118 42.388 74.927 3.451 1.00 35.94 A C ATOM 630 ND1 HIS A 118 42.077 76.560 4.871 1.00 39.19 A N ATOM 631 CE1 HIS A 118 41.800 75.434 5.505 1.00 35.71 A C ATOM 632 NE2 HIS A 118 41.978 74.427 4.668 1.00 30.44 A N ATOM 633 C HIS A 118 40.766 77.287 1.157 1.00 37.75 A C ATOM 634 O HIS A 118 39.608 77.083 1.509 1.00 37.21 A O ATOM 635 N HIS A 119 41.274 76.777 0.047 1.00 39.01 A N ATOM 636 CA HIS A 119 40.419 76.154 −0.948 1.00 40.69 A C ATOM 637 CB HIS A 119 40.705 76.716 −2.342 1.00 43.45 A C ATOM 638 CG HIS A 119 40.031 78.024 −2.609 1.00 43.38 A C ATOM 639 CD2 HIS A 119 39.996 78.803 −3.718 1.00 45.46 A C ATOM 640 ND1 HIS A 119 39.284 78.681 −1.656 1.00 48.21 A N ATOM 641 CE1 HIS A 119 38.811 79.806 −2.168 1.00 46.37 A C ATOM 642 NE2 HIS A 119 39.231 79.904 −3.415 1.00 49.26 A N ATOM 643 C HIS A 119 40.542 74.652 −0.969 1.00 36.19 A C ATOM 644 O HIS A 119 39.615 73.964 −1.389 1.00 34.90 A O ATOM 645 N ASN A 120 41.676 74.119 −0.542 1.00 34.14 A N ATOM 646 CA ASN A 120 41.753 72.673 −0.490 1.00 37.82 A C ATOM 647 CB ASN A 120 43.054 72.102 −1.036 1.00 39.91 A C ATOM 648 CG ASN A 120 43.004 70.585 −1.137 1.00 42.78 A C ATOM 649 OD1 ASN A 120 41.920 69.987 −1.147 1.00 41.85 A O ATOM 650 ND2 ASN A 120 44.168 69.952 −1.198 1.00 43.98 A N ATOM 651 C ASN A 120 41.492 72.159 0.902 1.00 38.56 A C ATOM 652 O ASN A 120 42.316 72.309 1.805 1.00 37.15 A O ATOM 653 N ILE A 121 40.324 71.552 1.062 1.00 36.47 A N ATOM 654 CA ILE A 121 39.860 71.125 2.367 1.00 35.04 A C ATOM 655 CB ILE A 121 38.342 71.363 2.486 1.00 35.92 A C ATOM 656 CG2 ILE A 121 37.870 71.234 3.931 1.00 32.74 A C ATOM 657 CG1 ILE A 121 37.999 72.752 1.926 1.00 34.55 A C ATOM 658 CD1 ILE A 121 38.622 73.893 2.721 1.00 32.69 A C ATOM 659 C ILE A 121 40.216 69.656 2.517 1.00 35.49 A C ATOM 660 O ILE A 121 39.942 68.845 1.634 1.00 37.37 A O ATOM 661 N THR A 122 40.886 69.322 3.608 1.00 33.32 A N ATOM 662 CA THR A 122 41.321 67.955 3.819 1.00 33.79 A C ATOM 663 CB THR A 122 42.725 67.915 4.405 1.00 31.56 A C ATOM 664 OG1 THR A 122 42.803 68.847 5.487 1.00 37.24 A O ATOM 665 CG2 THR A 122 43.736 68.330 3.339 1.00 37.38 A C ATOM 666 C THR A 122 40.345 67.304 4.774 1.00 33.11 A C ATOM 667 O THR A 122 39.784 67.965 5.637 1.00 33.85 A O ATOM 668 N TYR A 123 40.115 66.016 4.604 1.00 31.79 A N ATOM 669 CA TYR A 123 39.262 65.311 5.536 1.00 35.53 A C ATOM 670 CB TYR A 123 37.839 65.133 4.989 1.00 30.50 A C ATOM 671 CG TYR A 123 37.701 64.199 3.813 1.00 28.17 A C ATOM 672 CD1 TYR A 123 37.769 64.678 2.520 1.00 29.99 A C ATOM 673 CE1 TYR A 123 37.629 63.832 1.432 1.00 29.02 A C ATOM 674 CD2 TYR A 123 37.459 62.834 4.004 1.00 31.77 A C ATOM 675 CE2 TYR A 123 37.308 61.974 2.926 1.00 30.51 A C ATOM 676 CZ TYR A 123 37.395 62.486 1.638 1.00 33.72 A C ATOM 677 OH TYR A 123 37.247 61.656 0.547 1.00 31.89 A O ATOM 678 C TYR A 123 39.885 63.982 5.889 1.00 35.94 A C ATOM 679 O TYR A 123 40.608 63.393 5.080 1.00 34.12 A O ATOM 680 N TRP A 124 39.633 63.541 7.118 1.00 32.13 A N ATOM 681 CA TRP A 124 40.134 62.263 7.582 1.00 32.38 A C ATOM 682 CB TRP A 124 41.237 62.486 8.604 1.00 37.24 A C ATOM 683 CG TRP A 124 41.719 61.245 9.263 1.00 37.82 A C ATOM 684 CD2 TRP A 124 41.995 61.074 10.655 1.00 39.32 A C ATOM 685 CE2 TRP A 124 42.436 59.752 10.835 1.00 39.37 A C ATOM 686 CE3 TRP A 124 41.900 61.913 11.771 1.00 41.23 A C ATOM 687 CD1 TRP A 124 42.001 60.060 8.668 1.00 39.14 A C ATOM 688 NE1 TRP A 124 42.432 59.149 9.605 1.00 40.13 A N ATOM 689 CZ2 TRP A 124 42.789 59.245 12.080 1.00 41.73 A C ATOM 690 CZ3 TRP A 124 42.245 61.409 13.010 1.00 45.92 A C ATOM 691 CH2 TRP A 124 42.690 60.088 13.154 1.00 46.29 A C ATOM 692 C TRP A 124 39.006 61.419 8.159 1.00 33.61 A C ATOM 693 O TRP A 124 38.250 61.866 9.030 1.00 33.96 A O ATOM 694 N ILE A 125 38.884 60.203 7.645 1.00 32.03 A N ATOM 695 CA ILE A 125 37.904 59.247 8.145 1.00 34.71 A C ATOM 696 CB ILE A 125 37.492 58.241 7.043 1.00 35.73 A C ATOM 697 CG2 ILE A 125 36.565 57.177 7.599 1.00 32.66 A C ATOM 698 CG1 ILE A 125 36.843 58.989 5.877 1.00 33.43 A C ATOM 699 CD1 ILE A 125 36.917 58.248 4.566 1.00 38.78 A C ATOM 700 C ILE A 125 38.549 58.524 9.316 1.00 34.73 A C ATOM 701 O ILE A 125 39.291 57.555 9.133 1.00 34.48 A O ATOM 702 N GLN A 126 38.290 59.028 10.516 1.00 36.27 A N ATOM 703 CA GLN A 126 38.951 58.536 11.708 1.00 36.59 A C ATOM 704 CB GLN A 126 38.592 59.405 12.912 1.00 39.49 A C ATOM 705 CG GLN A 126 39.428 59.119 14.150 1.00 41.05 A C ATOM 706 CD GLN A 126 39.146 60.094 15.286 1.00 47.67 A C ATOM 707 OE1 GLN A 126 38.060 60.677 15.374 1.00 47.32 A O ATOM 708 NE2 GLN A 126 40.125 60.264 16.170 1.00 51.05 A N ATOM 709 C GLN A 126 38.578 57.083 11.949 1.00 38.71 A C ATOM 710 O GLN A 126 39.439 56.258 12.265 1.00 38.60 A O ATOM 711 N ASN A 127 37.302 56.760 11.768 1.00 33.96 A N ATOM 712 CA ASN A 127 36.851 55.387 11.938 1.00 35.25 A C ATOM 713 CB ASN A 127 36.582 55.102 13.423 1.00 36.32 A C ATOM 714 CG ASN A 127 35.470 55.974 13.996 1.00 38.35 A C ATOM 715 OD1 ASN A 127 34.929 56.842 13.312 1.00 36.26 A O ATOM 716 ND2 ASN A 127 35.123 55.739 15.259 1.00 38.22 A N ATOM 717 C ASN A 127 35.650 55.005 11.056 1.00 34.32 A C ATOM 718 O ASN A 127 35.150 55.817 10.280 1.00 33.29 A O ATOM 719 N TYR A 128 35.215 53.756 11.163 1.00 34.08 A N ATOM 720 CA TYR A 128 34.097 53.253 10.382 1.00 34.30 A C ATOM 721 CB TYR A 128 34.577 52.245 9.350 1.00 33.31 A C ATOM 722 CG TYR A 128 35.513 52.819 8.321 1.00 38.44 A C ATOM 723 CD1 TYR A 128 35.095 53.019 7.014 1.00 35.21 A C ATOM 724 CE1 TYR A 128 35.951 53.537 6.063 1.00 40.15 A C ATOM 725 CD2 TYR A 128 36.823 53.146 8.654 1.00 38.79 A C ATOM 726 CE2 TYR A 128 37.685 53.664 7.713 1.00 39.02 A C ATOM 727 CZ TYR A 128 37.243 53.860 6.418 1.00 39.96 A C ATOM 728 OH TYR A 128 38.098 54.374 5.477 1.00 38.78 A O ATOM 729 C TYR A 128 33.056 52.553 11.241 1.00 37.50 A C ATOM 730 O TYR A 128 33.391 51.911 12.229 1.00 39.58 A O ATOM 731 N SER A 129 31.793 52.664 10.833 1.00 33.63 A N ATOM 732 CA SER A 129 30.736 51.805 11.351 1.00 35.09 A C ATOM 733 CB SER A 129 29.369 52.442 11.109 1.00 30.54 A C ATOM 734 OG SER A 129 28.400 51.460 10.806 1.00 29.48 A O ATOM 735 C SER A 129 30.813 50.489 10.598 1.00 37.53 A C ATOM 736 O SER A 129 31.270 50.451 9.449 1.00 33.62 A O ATOM 737 N GLU A 130 30.345 49.415 11.222 1.00 34.80 A N ATOM 738 CA GLU A 130 30.433 48.100 10.605 1.00 35.34 A C ATOM 739 CB GLU A 130 30.740 47.039 11.659 1.00 40.30 A C ATOM 740 CG GLU A 130 31.972 47.364 12.508 1.00 38.06 A C ATOM 741 CD GLU A 130 33.270 47.212 11.738 1.00 45.15 A C ATOM 742 OE1 GLU A 130 33.239 46.639 10.623 1.00 44.01 A O ATOM 743 OE2 GLU A 130 34.324 47.654 12.254 1.00 50.94 A O ATOM 744 C GLU A 130 29.168 47.755 9.836 1.00 35.43 A C ATOM 745 O GLU A 130 29.002 46.627 9.376 1.00 31.50 A O ATOM 746 N ASP A 131 28.280 48.736 9.689 1.00 33.47 A N ATOM 747 CA ASP A 131 27.042 48.542 8.935 1.00 33.74 A C ATOM 748 CB ASP A 131 26.109 49.740 9.124 1.00 31.58 A C ATOM 749 CG ASP A 131 25.566 49.836 10.534 1.00 33.21 A C ATOM 750 OD1 ASP A 131 25.608 48.820 11.258 1.00 33.04 A O ATOM 751 OD2 ASP A 131 25.081 50.919 10.906 1.00 34.53 A O ATOM 752 C ASP A 131 27.270 48.323 7.435 1.00 32.07 A C ATOM 753 O ASP A 131 26.482 47.653 6.778 1.00 31.28 A O ATOM 754 N LEU A 132 28.330 48.917 6.902 1.00 30.54 A N ATOM 755 CA LEU A 132 28.610 48.888 5.461 1.00 33.69 A C ATOM 756 CB LEU A 132 28.348 50.269 4.856 1.00 33.34 A C ATOM 757 CG LEU A 132 26.899 50.762 4.777 1.00 36.27 A C ATOM 758 CD1 LEU A 132 26.813 52.295 4.611 1.00 30.58 A C ATOM 759 CD2 LEU A 132 26.179 50.045 3.637 1.00 34.05 A C ATOM 760 C LEU A 132 30.073 48.538 5.258 1.00 30.82 A C ATOM 761 O LEU A 132 30.872 48.727 6.171 1.00 31.95 A O ATOM 762 N PRO A 133 30.439 48.040 4.060 1.00 34.02 A N ATOM 763 CD PRO A 133 29.583 47.525 2.976 1.00 32.69 A C ATOM 764 CA PRO A 133 31.863 47.822 3.787 1.00 31.22 A C ATOM 765 CB PRO A 133 31.874 47.267 2.360 1.00 32.02 A C ATOM 766 CG PRO A 133 30.534 46.656 2.174 1.00 33.97 A C ATOM 767 C PRO A 133 32.599 49.148 3.838 1.00 35.28 A C ATOM 768 O PRO A 133 31.978 50.193 3.668 1.00 37.04 A O ATOM 769 N ARG A 134 33.906 49.115 4.062 1.00 34.27 A N ATOM 770 CA ARG A 134 34.649 50.350 4.254 1.00 34.85 A C ATOM 771 CB ARG A 134 36.015 50.056 4.860 1.00 38.63 A C ATOM 772 CG ARG A 134 35.980 49.663 6.335 1.00 41.61 A C ATOM 773 CD ARG A 134 37.396 49.406 6.835 1.00 44.68 A C ATOM 774 NE ARG A 134 37.490 49.388 8.289 1.00 52.21 A N ATOM 775 CZ ARG A 134 38.615 49.618 8.957 1.00 51.24 A C ATOM 776 NH1 ARG A 134 39.735 49.897 8.296 1.00 51.17 A N ATOM 777 NH2 ARG A 134 38.618 49.587 10.285 1.00 54.94 A N ATOM 778 C ARG A 134 34.798 51.118 2.941 1.00 35.98 A C ATOM 779 O ARG A 134 34.914 52.348 2.931 1.00 35.27 A O ATOM 780 N ALA A 135 34.796 50.388 1.833 1.00 34.04 A N ATOM 781 CA ALA A 135 34.886 51.009 0.518 1.00 34.41 A C ATOM 782 CB ALA A 135 35.159 49.960 −0.531 1.00 41.14 A C ATOM 783 C ALA A 135 33.603 51.760 0.196 1.00 34.90 A C ATOM 784 O ALA A 135 33.624 52.844 −0.374 1.00 34.07 A O ATOM 785 N VAL A 136 32.480 51.164 0.571 1.00 35.75 A N ATOM 786 CA VAL A 136 31.188 51.783 0.356 1.00 35.31 A C ATOM 787 CB VAL A 136 30.057 50.793 0.657 1.00 36.15 A C ATOM 788 CG1 VAL A 136 28.723 51.502 0.708 1.00 36.65 A C ATOM 789 CG2 VAL A 136 30.050 49.685 −0.403 1.00 32.23 A C ATOM 790 C VAL A 136 31.067 53.061 1.184 1.00 32.70 A C ATOM 791 O VAL A 136 30.537 54.063 0.713 1.00 35.23 A O ATOM 792 N ILE A 137 31.596 53.025 2.401 1.00 34.13 A N ATOM 793 CA ILE A 137 31.633 54.195 3.278 1.00 30.87 A C ATOM 794 CB ILE A 137 32.093 53.805 4.696 1.00 31.26 A C ATOM 795 CG2 ILE A 137 32.497 55.048 5.490 1.00 29.94 A C ATOM 796 CG1 ILE A 137 30.989 53.014 5.416 1.00 32.05 A C ATOM 797 CD1 ILE A 137 31.308 52.643 6.871 1.00 31.59 A C ATOM 798 C ILE A 137 32.551 55.297 2.730 1.00 33.59 A C ATOM 799 O ILE A 137 32.182 56.487 2.705 1.00 30.17 A O ATOM 800 N ASP A 138 33.747 54.900 2.307 1.00 30.00 A N ATOM 801 CA ASP A 138 34.659 55.801 1.609 1.00 32.34 A C ATOM 802 CB ASP A 138 35.874 55.030 1.097 1.00 33.62 A C ATOM 803 CG ASP A 138 36.824 54.607 2.216 1.00 38.02 A C ATOM 804 OD1 ASP A 138 36.583 54.934 3.400 1.00 38.89 A O ATOM 805 OD2 ASP A 138 37.825 53.943 1.902 1.00 42.12 A O ATOM 806 C ASP A 138 33.985 56.511 0.432 1.00 29.33 A C ATOM 807 O ASP A 138 34.087 57.722 0.286 1.00 27.63 A O ATOM 808 N ASP A 139 33.288 55.752 −0.400 1.00 28.62 A N ATOM 809 CA ASP A 139 32.706 56.307 −1.613 1.00 28.03 A C ATOM 810 CB ASP A 139 32.306 55.181 −2.567 1.00 32.93 A C ATOM 811 CG ASP A 139 31.431 55.661 −3.713 1.00 34.02 A C ATOM 812 OD1 ASP A 139 31.945 56.360 −4.614 1.00 35.82 A O ATOM 813 OD2 ASP A 139 30.231 55.323 −3.718 1.00 33.21 A O ATOM 814 C ASP A 139 31.501 57.190 −1.286 1.00 31.06 A C ATOM 815 O ASP A 139 31.251 58.192 −1.971 1.00 27.48 A O ATOM 816 N ALA A 140 30.757 56.820 −0.240 1.00 27.86 A N ATOM 817 CA ALA A 140 29.629 57.639 0.196 1.00 28.33 A C ATOM 818 CB ALA A 140 28.887 56.980 1.388 1.00 27.35 A C ATOM 819 C ALA A 140 30.114 59.033 0.568 1.00 28.15 A C ATOM 820 O ALA A 140 29.503 60.030 0.206 1.00 30.28 A O ATOM 821 N PHE A 141 31.215 59.104 1.306 1.00 25.19 A N ATOM 822 CA PHE A 141 31.743 60.385 1.751 1.00 26.39 A C ATOM 823 CB PHE A 141 32.824 60.184 2.824 1.00 27.84 A C ATOM 824 CG PHE A 141 32.284 59.786 4.167 1.00 27.54 A C ATOM 825 CD1 PHE A 141 31.086 60.310 4.636 1.00 28.49 A C ATOM 826 CD2 PHE A 141 32.984 58.913 4.977 1.00 26.64 A C ATOM 827 CE1 PHE A 141 30.591 59.954 5.883 1.00 25.61 A C ATOM 828 CE2 PHE A 141 32.494 58.554 6.213 1.00 30.05 A C ATOM 829 CZ PHE A 141 31.290 59.078 6.664 1.00 25.09 A C ATOM 830 C PHE A 141 32.324 61.177 0.582 1.00 26.34 A C ATOM 831 O PHE A 141 32.151 62.397 0.481 1.00 25.43 A O ATOM 832 N ALA A 142 33.030 60.469 −0.293 1.00 28.11 A N ATOM 833 CA ALA A 142 33.593 61.072 −1.498 1.00 29.78 A C ATOM 834 CB ALA A 142 34.308 59.996 −2.340 1.00 28.59 A C ATOM 835 C ALA A 142 32.474 61.730 −2.295 1.00 24.71 A C ATOM 836 O ALA A 142 32.543 62.900 −2.659 1.00 26.50 A O ATOM 837 N ARG A 143 31.419 60.971 −2.540 1.00 26.34 A N ATOM 838 CA ARG A 143 30.325 61.466 −3.367 1.00 24.57 A C ATOM 839 CB ARG A 143 29.364 60.335 −3.686 1.00 26.29 A C ATOM 840 CG ARG A 143 30.017 59.278 −4.561 1.00 26.65 A C ATOM 841 CD ARG A 143 29.281 57.954 −4.562 1.00 32.59 A C ATOM 842 NE ARG A 143 27.856 58.180 −4.577 1.00 39.33 A N ATOM 843 CZ ARG A 143 26.986 57.684 −3.704 1.00 32.38 A C ATOM 844 NH1 ARG A 143 27.368 56.864 −2.736 1.00 35.65 A N ATOM 845 NH2 ARG A 143 25.712 57.992 −3.838 1.00 26.09 A N ATOM 846 C ARG A 143 29.637 62.657 −2.715 1.00 25.78 A C ATOM 847 O ARG A 143 29.191 63.577 −3.400 1.00 25.47 A O ATOM 848 N ALA A 144 29.578 62.649 −1.384 1.00 26.55 A N ATOM 849 CA ALA A 144 28.950 63.732 −0.640 1.00 27.17 A C ATOM 850 CB ALA A 144 28.826 63.374 0.849 1.00 23.15 A C ATOM 851 C ALA A 144 29.744 65.029 −0.827 1.00 28.05 A C ATOM 852 O ALA A 144 29.153 66.095 −1.026 1.00 27.61 A O ATOM 853 N PHE A 145 31.075 64.926 −0.762 1.00 25.94 A N ATOM 854 CA PHE A 145 31.958 66.064 −1.033 1.00 25.40 A C ATOM 855 CB PHE A 145 33.420 65.782 −0.635 1.00 23.53 A C ATOM 856 CG PHE A 145 33.691 65.850 0.877 1.00 26.68 A C ATOM 857 CD1 PHE A 145 33.483 67.020 1.588 1.00 29.09 A C ATOM 858 CD2 PHE A 145 34.198 64.746 1.557 1.00 24.57 A C ATOM 859 CE1 PHE A 145 33.729 67.079 2.993 1.00 30.37 A C ATOM 860 CE2 PHE A 145 34.471 64.795 2.930 1.00 28.66 A C ATOM 861 CZ PHE A 145 34.241 65.971 3.649 1.00 27.25 A C ATOM 862 C PHE A 145 31.899 66.479 −2.502 1.00 26.99 A C ATOM 863 O PHE A 145 31.940 67.670 −2.819 1.00 25.55 A O ATOM 864 N ALA A 146 31.803 65.503 −3.401 1.00 24.15 A N ATOM 865 CA ALA A 146 31.693 65.841 −4.820 1.00 27.56 A C ATOM 866 CB ALA A 146 31.648 64.601 −5.672 1.00 22.76 A C ATOM 867 C ALA A 146 30.492 66.748 −5.112 1.00 28.12 A C ATOM 868 O ALA A 146 30.508 67.502 −6.081 1.00 27.69 A O ATOM 869 N LEU A 147 29.449 66.682 −4.288 1.00 24.01 A N ATOM 870 CA LEU A 147 28.294 67.562 −4.486 1.00 26.95 A C ATOM 871 CB LEU A 147 27.175 67.242 −3.487 1.00 22.66 A C ATOM 872 CG LEU A 147 26.432 65.923 −3.640 1.00 26.53 A C ATOM 873 CD1 LEU A 147 25.598 65.655 −2.375 1.00 26.10 A C ATOM 874 CD2 LEU A 147 25.548 65.957 −4.887 1.00 23.87 A C ATOM 875 C LEU A 147 28.665 69.020 −4.299 1.00 26.94 A C ATOM 876 O LEU A 147 28.211 69.885 −5.035 1.00 28.14 A O ATOM 877 N TRP A 148 29.451 69.288 −3.265 1.00 26.18 A N ATOM 878 CA TRP A 148 29.809 70.649 −2.903 1.00 28.26 A C ATOM 879 CB TRP A 148 30.171 70.724 −1.415 1.00 26.25 A C ATOM 880 CG TRP A 148 29.025 70.384 −0.462 1.00 29.47 A C ATOM 881 CD2 TRP A 148 27.813 71.129 −0.269 1.00 25.31 A C ATOM 882 CE2 TRP A 148 27.053 70.451 0.715 1.00 25.37 A C ATOM 883 CE3 TRP A 148 27.291 72.303 −0.828 1.00 24.79 A C ATOM 884 CD1 TRP A 148 28.956 69.317 0.393 1.00 27.04 A C ATOM 885 NE1 TRP A 148 27.768 69.340 1.090 1.00 25.97 A N ATOM 886 CZ2 TRP A 148 25.803 70.903 1.145 1.00 22.37 A C ATOM 887 CZ3 TRP A 148 26.046 72.751 −0.401 1.00 26.23 A C ATOM 888 CH2 TRP A 148 25.321 72.053 0.576 1.00 24.80 A C ATOM 889 C TRP A 148 30.978 71.194 −3.748 1.00 29.42 A C ATOM 890 O TRP A 148 31.034 72.386 −4.052 1.00 30.04 A O ATOM 891 N SER A 149 31.921 70.343 −4.128 1.00 28.30 A N ATOM 892 CA SER A 149 33.024 70.868 −4.919 1.00 30.08 A C ATOM 893 CB SER A 149 34.150 69.843 −5.134 1.00 32.03 A C ATOM 894 OG SER A 149 33.707 68.744 −5.887 1.00 31.75 A O ATOM 895 C SER A 149 32.535 71.421 −6.249 1.00 29.70 A C ATOM 896 O SER A 149 33.095 72.389 −6.746 1.00 31.03 A O ATOM 897 N ALA A 150 31.482 70.834 −6.814 1.00 26.31 A N ATOM 898 CA ALA A 150 31.052 71.244 −8.144 1.00 27.35 A C ATOM 899 CB ALA A 150 30.107 70.225 −8.765 1.00 25.89 A C ATOM 900 C ALA A 150 30.422 72.619 −8.129 1.00 26.34 A C ATOM 901 O ALA A 150 30.343 73.274 −9.158 1.00 28.56 A O ATOM 902 N VAL A 151 29.982 73.068 −6.963 1.00 30.71 A N ATOM 903 CA VAL A 151 29.254 74.331 −6.870 1.00 26.68 A C ATOM 904 CB VAL A 151 27.846 74.127 −6.289 1.00 28.01 A C ATOM 905 CG1 VAL A 151 26.943 73.412 −7.310 1.00 21.35 A C ATOM 906 CG2 VAL A 151 27.908 73.364 −4.975 1.00 24.95 A C ATOM 907 C VAL A 151 30.006 75.365 −6.039 1.00 28.35 A C ATOM 908 O VAL A 151 29.472 76.423 −5.731 1.00 28.96 A O ATOM 909 N THR A 152 31.241 75.038 −5.668 1.00 31.04 A N ATOM 910 CA THR A 152 32.107 75.949 −4.920 1.00 33.79 A C ATOM 911 CB THR A 152 32.363 75.449 −3.494 1.00 32.22 A C ATOM 912 OG1 THR A 152 33.046 74.193 −3.566 1.00 33.57 A O ATOM 913 CG2 THR A 152 31.076 75.290 −2.704 1.00 31.46 A C ATOM 914 C THR A 152 33.492 75.977 −5.553 1.00 32.36 A C ATOM 915 O THR A 152 33.837 75.101 −6.349 1.00 31.69 A O ATOM 916 N PRO A 153 34.302 76.970 −5.172 1.00 33.49 A N ATOM 917 CD PRO A 153 33.901 78.188 −4.442 1.00 35.31 A C ATOM 918 CA PRO A 153 35.715 77.001 −5.540 1.00 35.09 A C ATOM 919 CB PRO A 153 36.063 78.477 −5.401 1.00 38.04 A C ATOM 920 CG PRO A 153 35.194 78.942 −4.299 1.00 37.03 A C ATOM 921 C PRO A 153 36.543 76.198 −4.551 1.00 38.62 A C ATOM 922 O PRO A 153 37.699 76.546 −4.303 1.00 42.36 A O ATOM 923 N LEU A 154 35.963 75.137 −3.997 1.00 35.00 A N ATOM 924 CA LEU A 154 36.654 74.310 −3.017 1.00 32.10 A C ATOM 925 CB LEU A 154 35.780 74.137 −1.761 1.00 32.47 A C ATOM 926 CG LEU A 154 35.470 75.386 −0.943 1.00 31.94 A C ATOM 927 CD1 LEU A 154 34.597 75.051 0.270 1.00 30.62 A C ATOM 928 CD2 LEU A 154 36.745 76.050 −0.488 1.00 34.26 A C ATOM 929 C LEU A 154 36.986 72.946 −3.593 1.00 28.38 A C ATOM 930 O LEU A 154 36.322 72.473 −4.506 1.00 30.89 A O ATOM 931 N THR A 155 38.021 72.317 −3.060 1.00 27.70 A N ATOM 932 CA THR A 155 38.337 70.936 −3.388 1.00 31.65 A C ATOM 933 CB THR A 155 39.693 70.782 −4.127 1.00 33.47 A C ATOM 934 OG1 THR A 155 40.755 71.266 −3.286 1.00 34.93 A O ATOM 935 CG2 THR A 155 39.676 71.549 −5.432 1.00 30.56 A C ATOM 936 C THR A 155 38.455 70.170 −2.083 1.00 30.71 A C ATOM 937 O THR A 155 38.745 70.744 −1.039 1.00 31.54 A O ATOM 938 N PHE A 156 38.246 68.867 −2.148 1.00 30.93 A N ATOM 939 CA PHE A 156 38.257 68.055 −0.958 1.00 31.65 A C ATOM 940 CB PHE A 156 36.837 67.566 −0.638 1.00 29.40 A C ATOM 941 CG PHE A 156 35.862 68.688 −0.436 1.00 28.75 A C ATOM 942 CD1 PHE A 156 34.955 69.028 −1.424 1.00 27.60 A C ATOM 943 CD2 PHE A 156 35.877 69.429 0.739 1.00 27.89 A C ATOM 944 CE1 PHE A 156 34.068 70.077 −1.239 1.00 25.20 A C ATOM 945 CE2 PHE A 156 35.015 70.486 0.919 1.00 26.59 A C ATOM 946 CZ PHE A 156 34.102 70.804 −0.067 1.00 26.89 A C ATOM 947 C PHE A 156 39.206 66.911 −1.183 1.00 33.31 A C ATOM 948 O PHE A 156 39.109 66.190 −2.170 1.00 34.85 A O ATOM 949 N THR A 157 40.133 66.746 −0.258 1.00 30.73 A N ATOM 950 CA THR A 157 41.157 65.747 −0.428 1.00 34.40 A C ATOM 951 CB THR A 157 42.522 66.429 −0.613 1.00 38.71 A C ATOM 952 OG1 THR A 157 42.463 67.319 −1.739 1.00 35.38 A O ATOM 953 CG2 THR A 157 43.606 65.396 −0.833 1.00 41.42 A C ATOM 954 C THR A 157 41.191 64.867 0.806 1.00 34.77 A C ATOM 955 O THR A 157 41.279 65.368 1.920 1.00 34.87 A O ATOM 956 N ARG A 158 41.119 63.558 0.612 1.00 34.19 A N ATOM 957 CA ARG A 158 41.209 62.640 1.743 1.00 38.15 A C ATOM 958 CB ARG A 158 40.718 61.253 1.338 1.00 34.77 A C ATOM 959 CG ARG A 158 40.683 60.268 2.485 1.00 38.04 A C ATOM 960 CD ARG A 158 40.314 58.890 1.997 1.00 37.91 A C ATOM 961 NE ARG A 158 40.310 57.924 3.095 1.00 41.14 A N ATOM 962 CZ ARG A 158 40.014 56.638 2.947 1.00 38.65 A C ATOM 963 NH1 ARG A 158 39.692 56.170 1.746 1.00 40.42 A N ATOM 964 NH2 ARG A 158 40.034 55.825 4.001 1.00 40.15 A N ATOM 965 C ARG A 158 42.642 62.569 2.291 1.00 39.05 A C ATOM 966 O ARG A 158 43.604 62.473 1.525 1.00 38.61 A O ATOM 967 N VAL A 159 42.778 62.652 3.614 1.00 39.33 A N ATOM 968 CA VAL A 159 44.079 62.494 4.280 1.00 39.96 A C ATOM 969 CB VAL A 159 44.560 63.800 4.942 1.00 38.47 A C ATOM 970 CG1 VAL A 159 44.853 64.863 3.896 1.00 36.99 A C ATOM 971 CG2 VAL A 159 43.532 64.302 5.973 1.00 40.99 A C ATOM 972 C VAL A 159 43.997 61.425 5.369 1.00 43.78 A C ATOM 973 O VAL A 159 42.917 60.887 5.648 1.00 42.78 A O ATOM 974 N TYR A 160 45.126 61.134 6.008 1.00 42.14 A N ATOM 975 CA TYR A 160 45.129 60.140 7.080 1.00 42.71 A C ATOM 976 CB TYR A 160 45.792 58.846 6.606 1.00 40.59 A C ATOM 977 CG TYR A 160 45.100 58.241 5.395 1.00 40.66 A C ATOM 978 CD1 TYR A 160 45.296 58.770 4.117 1.00 39.02 A C ATOM 979 CE1 TYR A 160 44.662 58.227 3.010 1.00 36.95 A C ATOM 980 CD2 TYR A 160 44.254 57.146 5.531 1.00 38.87 A C ATOM 981 CE2 TYR A 160 43.618 56.597 4.435 1.00 42.17 A C ATOM 982 CZ TYR A 160 43.824 57.140 3.179 1.00 39.77 A C ATOM 983 OH TYR A 160 43.188 56.594 2.097 1.00 44.98 A O ATOM 984 C TYR A 160 45.772 60.659 8.362 1.00 43.54 A C ATOM 985 O TYR A 160 46.701 60.055 8.890 1.00 53.85 A O ATOM 986 N SER A 161 45.262 61.775 8.872 1.00 47.07 A N ATOM 987 CA SER A 161 45.821 62.384 10.075 1.00 46.44 A C ATOM 988 CB SER A 161 47.077 63.178 9.722 1.00 49.30 A C ATOM 989 OG SER A 161 46.739 64.371 9.033 1.00 53.70 A O ATOM 990 C SER A 161 44.832 63.289 10.821 1.00 49.42 A C ATOM 991 O SER A 161 43.772 63.645 10.302 1.00 47.62 A O ATOM 992 N ARG A 162 45.206 63.680 12.035 1.00 48.06 A N ATOM 993 CA ARG A 162 44.319 64.403 12.932 1.00 46.94 A C ATOM 994 CB ARG A 162 44.779 64.225 14.386 1.00 53.10 A C ATOM 995 CG ARG A 162 45.835 65.229 14.844 1.00 56.44 A C ATOM 996 CD ARG A 162 46.288 64.968 16.287 1.00 59.83 A C ATOM 997 NE ARG A 162 47.255 63.874 16.349 1.00 61.82 A N ATOM 998 CZ ARG A 162 48.545 64.006 16.059 1.00 56.43 A C ATOM 999 NH1 ARG A 162 49.356 62.955 16.130 1.00 55.31 A N ATOM 1000 NH2 ARG A 162 49.025 65.192 15.697 1.00 53.51 A N ATOM 1001 C ARG A 162 44.179 65.893 12.610 1.00 48.76 A C ATOM 1002 O ARG A 162 43.301 66.569 13.153 1.00 53.29 A O ATOM 1003 N ASP A 163 45.039 66.417 11.745 1.00 47.82 A N ATOM 1004 CA ASP A 163 44.948 67.834 11.384 1.00 49.50 A C ATOM 1005 CB ASP A 163 46.330 68.480 11.369 1.00 49.08 A C ATOM 1006 CG ASP A 163 47.114 68.103 10.135 1.00 58.58 A C ATOM 1007 OD1 ASP A 163 47.080 66.898 9.772 1.00 58.06 A O ATOM 1008 OD2 ASP A 163 47.738 69.002 9.519 1.00 61.81 A O ATOM 1009 C ASP A 163 44.280 68.058 10.019 1.00 47.10 A C ATOM 1010 O ASP A 163 44.539 69.063 9.348 1.00 44.34 A O ATOM 1011 N ALA A 164 43.447 67.112 9.598 1.00 43.21 A N ATOM 1012 CA ALA A 164 42.572 67.345 8.462 1.00 34.44 A C ATOM 1013 CB ALA A 164 41.751 66.114 8.198 1.00 34.77 A C ATOM 1014 C ALA A 164 41.672 68.486 8.888 1.00 34.58 A C ATOM 1015 O ALA A 164 41.419 68.646 10.082 1.00 33.55 A O ATOM 1016 N ASP A 165 41.189 69.286 7.944 1.00 33.90 A N ATOM 1017 CA ASP A 165 40.210 70.322 8.291 1.00 30.64 A C ATOM 1018 CB ASP A 165 39.854 71.163 7.077 1.00 33.40 A C ATOM 1019 CG ASP A 165 41.060 71.862 6.482 1.00 34.70 A C ATOM 1020 OD1 ASP A 165 41.752 72.581 7.242 1.00 32.19 A O ATOM 1021 OD2 ASP A 165 41.306 71.687 5.267 1.00 30.63 A O ATOM 1022 C ASP A 165 38.941 69.676 8.808 1.00 34.73 A C ATOM 1023 O ASP A 165 38.314 70.158 9.766 1.00 32.92 A O ATOM 1024 N ILE A 166 38.555 68.591 8.150 1.00 28.96 A N ATOM 1025 CA ILE A 166 37.350 67.879 8.509 1.00 34.84 A C ATOM 1026 CB ILE A 166 36.383 67.809 7.299 1.00 33.41 A C ATOM 1027 CG2 ILE A 166 35.080 67.090 7.685 1.00 31.92 A C ATOM 1028 CG1 ILE A 166 36.129 69.229 6.767 1.00 33.20 A C ATOM 1029 CD1 ILE A 166 35.057 69.339 5.714 1.00 29.85 A C ATOM 1030 C ILE A 166 37.683 66.481 9.018 1.00 33.17 A C ATOM 1031 O ILE A 166 38.100 65.624 8.250 1.00 33.02 A O ATOM 1032 N VAL A 167 37.526 66.262 10.319 1.00 35.82 A N ATOM 1033 CA VAL A 167 37.659 64.916 10.866 1.00 31.91 A C ATOM 1034 CB VAL A 167 38.362 64.892 12.238 1.00 37.58 A C ATOM 1035 CG1 VAL A 167 38.541 63.448 12.704 1.00 34.82 A C ATOM 1036 CG2 VAL A 167 39.714 65.619 12.175 1.00 30.53 A C ATOM 1037 C VAL A 167 36.276 64.260 10.935 1.00 31.08 A C ATOM 1038 O VAL A 167 35.310 64.844 11.423 1.00 34.21 A O ATOM 1039 N ILE A 168 36.191 63.052 10.403 1.00 31.53 A N ATOM 1040 CA ILE A 168 34.930 62.341 10.284 1.00 31.98 A C ATOM 1041 CB ILE A 168 34.712 61.845 8.840 1.00 31.48 A C ATOM 1042 CG2 ILE A 168 33.650 60.751 8.800 1.00 31.96 A C ATOM 1043 CG1 ILE A 168 34.348 63.024 7.928 1.00 29.33 A C ATOM 1044 CD1 ILE A 168 34.362 62.690 6.436 1.00 31.27 A C ATOM 1045 C ILE A 168 34.965 61.160 11.236 1.00 33.80 A C ATOM 1046 O ILE A 168 35.932 60.391 11.247 1.00 31.48 A O ATOM 1047 N GLN A 169 33.899 61.013 12.016 1.00 32.50 A N ATOM 1048 CA GLN A 169 33.888 60.076 13.133 1.00 34.79 A C ATOM 1049 CB GLN A 169 34.226 60.846 14.413 1.00 32.85 A C ATOM 1050 CG GLN A 169 34.437 59.999 15.616 1.00 42.87 A C ATOM 1051 CD GLN A 169 34.611 60.831 16.873 1.00 46.03 A C ATOM 1052 OE1 GLN A 169 35.542 61.631 16.979 1.00 49.22 A O ATOM 1053 NE2 GLN A 169 33.707 60.648 17.828 1.00 41.49 A N ATOM 1054 C GLN A 169 32.541 59.377 13.298 1.00 30.90 A C ATOM 1055 O GLN A 169 31.493 60.005 13.182 1.00 32.96 A O ATOM 1056 N PHE A 170 32.565 58.076 13.565 1.00 28.24 A N ATOM 1057 CA PHE A 170 31.347 57.367 13.941 1.00 33.32 A C ATOM 1058 CB PHE A 170 31.269 56.002 13.262 1.00 31.41 A C ATOM 1059 CG PHE A 170 30.957 56.069 11.796 1.00 35.15 A C ATOM 1060 CD1 PHE A 170 31.965 56.268 10.862 1.00 32.14 A C ATOM 1061 CD2 PHE A 170 29.654 55.934 11.347 1.00 31.39 A C ATOM 1062 CE1 PHE A 170 31.671 56.333 9.511 1.00 33.22 A C ATOM 1063 CE2 PHE A 170 29.358 55.995 9.999 1.00 32.96 A C ATOM 1064 CZ PHE A 170 30.367 56.202 9.077 1.00 31.83 A C ATOM 1065 C PHE A 170 31.386 57.209 15.458 1.00 35.88 A C ATOM 1066 O PHE A 170 32.410 56.811 16.007 1.00 36.15 A O ATOM 1067 N GLY A 171 30.293 57.548 16.131 1.00 33.47 A N ATOM 1068 CA GLY A 171 30.241 57.478 17.585 1.00 35.91 A C ATOM 1069 C GLY A 171 28.854 57.173 18.151 1.00 36.90 A C ATOM 1070 O GLY A 171 27.850 57.240 17.431 1.00 36.90 A O ATOM 1071 N VAL A 172 28.805 56.819 19.437 1.00 34.80 A N ATOM 1072 CA VAL A 172 27.549 56.587 20.141 1.00 35.62 A C ATOM 1073 CB VAL A 172 27.295 55.086 20.379 1.00 37.59 A C ATOM 1074 CG1 VAL A 172 27.308 54.319 19.059 1.00 36.47 A C ATOM 1075 CG2 VAL A 172 28.327 54.527 21.335 1.00 38.39 A C ATOM 1076 C VAL A 172 27.558 57.293 21.498 1.00 39.36 A C ATOM 1077 O VAL A 172 28.621 57.546 22.065 1.00 38.19 A O ATOM 1078 N ALA A 173 26.372 57.594 22.019 1.00 35.84 A N ATOM 1079 CA ALA A 173 26.258 58.277 23.298 1.00 41.56 A C ATOM 1080 CB ALA A 173 26.413 57.284 24.457 1.00 39.79 A C ATOM 1081 C ALA A 173 27.321 59.363 23.377 1.00 43.55 A C ATOM 1082 O ALA A 173 27.575 60.058 22.385 1.00 39.83 A O ATOM 1083 N GLU A 174 27.942 59.510 24.545 1.00 39.85 A N ATOM 1084 CA GLU A 174 29.050 60.452 24.679 1.00 43.16 A C ATOM 1085 CB GLU A 174 29.381 60.731 26.144 1.00 45.98 A C ATOM 1086 CG GLU A 174 30.730 61.438 26.320 1.00 44.58 A C ATOM 1087 CD GLU A 174 30.749 62.827 25.709 1.00 44.52 A C ATOM 1088 OE1 GLU A 174 29.670 63.454 25.618 1.00 45.71 A O ATOM 1089 OE2 GLU A 174 31.847 63.297 25.328 1.00 49.52 A O ATOM 1090 C GLU A 174 30.292 59.926 23.959 1.00 42.18 A C ATOM 1091 O GLU A 174 30.823 58.865 24.290 1.00 40.68 A O ATOM 1092 N HIS A 175 30.762 60.679 22.979 1.00 43.41 A N ATOM 1093 CA HIS A 175 31.829 60.194 22.115 1.00 40.96 A C ATOM 1094 CB HIS A 175 31.276 59.923 20.729 1.00 39.18 A C ATOM 1095 CG HIS A 175 30.469 61.055 20.195 1.00 38.03 A C ATOM 1096 CD2 HIS A 175 30.781 62.047 19.334 1.00 38.32 A C ATOM 1097 ND1 HIS A 175 29.165 61.281 20.587 1.00 37.38 A N ATOM 1098 CE1 HIS A 175 28.708 62.354 19.975 1.00 39.65 A C ATOM 1099 NE2 HIS A 175 29.666 62.835 19.202 1.00 38.69 A N ATOM 1100 C HIS A 175 32.968 61.189 22.023 1.00 40.28 A C ATOM 1101 O HIS A 175 33.709 61.200 21.046 1.00 45.67 A O ATOM 1102 N GLY A 176 33.088 62.039 23.035 1.00 45.00 A N ATOM 1103 CA GLY A 176 34.286 62.831 23.212 1.00 44.18 A C ATOM 1104 C GLY A 176 34.173 64.324 22.994 1.00 41.52 A C ATOM 1105 O GLY A 176 35.176 65.021 23.087 1.00 39.80 A O ATOM 1106 N ASP A 177 32.976 64.833 22.711 1.00 41.99 A N ATOM 1107 CA ASP A 177 32.851 66.255 22.375 1.00 42.50 A C ATOM 1108 CB ASP A 177 32.550 66.453 20.880 1.00 44.74 A C ATOM 1109 CG ASP A 177 31.155 65.961 20.478 1.00 42.23 A C ATOM 1110 OD1 ASP A 177 30.459 65.334 21.302 1.00 40.45 A O ATOM 1111 OD2 ASP A 177 30.735 66.213 19.332 1.00 41.47 A O ATOM 1112 C ASP A 177 31.823 66.986 23.231 1.00 46.14 A C ATOM 1113 O ASP A 177 31.587 68.182 23.048 1.00 48.27 A O ATOM 1114 N GLY A 178 31.210 66.266 24.166 1.00 46.00 A N ATOM 1115 CA GLY A 178 30.233 66.874 25.057 1.00 43.88 A C ATOM 1116 C GLY A 178 28.883 67.151 24.411 1.00 44.06 A C ATOM 1117 O GLY A 178 28.060 67.876 24.965 1.00 45.44 A O ATOM 1118 N TYR A 179 28.660 66.580 23.233 1.00 43.05 A N ATOM 1119 CA TYR A 179 27.355 66.614 22.591 1.00 39.95 A C ATOM 1120 CB TYR A 179 27.400 67.459 21.322 1.00 43.11 A C ATOM 1121 CG TYR A 179 27.877 68.870 21.570 1.00 45.00 A C ATOM 1122 CD1 TYR A 179 29.188 69.245 21.289 1.00 47.83 A C ATOM 1123 CE1 TYR A 179 29.631 70.536 21.523 1.00 46.10 A C ATOM 1124 CD2 TYR A 179 27.021 69.824 22.106 1.00 44.61 A C ATOM 1125 CE2 TYR A 179 27.447 71.109 22.337 1.00 46.06 A C ATOM 1126 CZ TYR A 179 28.749 71.462 22.048 1.00 48.11 A C ATOM 1127 OH TYR A 179 29.165 72.750 22.287 1.00 53.97 A O ATOM 1128 C TYR A 179 26.988 65.174 22.271 1.00 42.03 A C ATOM 1129 O TYR A 179 27.153 64.715 21.136 1.00 39.70 A O ATOM 1130 N PRO A 180 26.495 64.444 23.280 1.00 39.35 A N ATOM 1131 CD PRO A 180 25.972 64.936 24.567 1.00 42.30 A C ATOM 1132 CA PRO A 180 26.338 62.994 23.139 1.00 38.35 A C ATOM 1133 CB PRO A 180 25.968 62.530 24.562 1.00 41.56 A C ATOM 1134 CG PRO A 180 26.147 63.743 25.461 1.00 45.95 A C ATOM 1135 C PRO A 180 25.211 62.665 22.184 1.00 37.72 A C ATOM 1136 O PRO A 180 24.266 63.438 22.060 1.00 32.68 A O ATOM 1137 N PHE A 181 25.317 61.535 21.503 1.00 37.23 A N ATOM 1138 CA PHE A 181 24.197 61.035 20.724 1.00 36.91 A C ATOM 1139 CB PHE A 181 24.689 60.083 19.634 1.00 35.63 A C ATOM 1140 CG PHE A 181 25.430 60.774 18.542 1.00 34.95 A C ATOM 1141 CD1 PHE A 181 24.921 61.939 17.981 1.00 37.36 A C ATOM 1142 CD2 PHE A 181 26.635 60.278 18.071 1.00 35.33 A C ATOM 1143 CE1 PHE A 181 25.607 62.594 16.958 1.00 34.44 A C ATOM 1144 CE2 PHE A 181 27.315 60.926 17.058 1.00 33.31 A C ATOM 1145 CZ PHE A 181 26.800 62.086 16.500 1.00 33.04 A C ATOM 1146 C PHE A 181 23.136 60.382 21.623 1.00 40.57 A C ATOM 1147 O PHE A 181 23.381 60.131 22.810 1.00 35.96 A O ATOM 1148 N ASP A 182 21.970 60.110 21.042 1.00 38.52 A N ATOM 1149 CA ASP A 182 20.765 59.796 21.805 1.00 40.16 A C ATOM 1150 CB ASP A 182 19.663 60.785 21.425 1.00 38.60 A C ATOM 1151 CG ASP A 182 19.304 60.713 19.947 1.00 40.33 A C ATOM 1152 OD1 ASP A 182 20.083 60.126 19.172 1.00 40.53 A O ATOM 1153 OD2 ASP A 182 18.259 61.250 19.546 1.00 40.77 A O ATOM 1154 C ASP A 182 20.242 58.380 21.558 1.00 41.02 A C ATOM 1155 O ASP A 182 19.026 58.150 21.601 1.00 41.40 A O ATOM 1156 N GLY A 183 21.141 57.436 21.292 1.00 38.85 A N ATOM 1157 CA GLY A 183 20.729 56.076 20.994 1.00 38.06 A C ATOM 1158 C GLY A 183 20.014 56.034 19.662 1.00 40.81 A C ATOM 1159 O GLY A 183 20.248 56.878 18.825 1.00 39.76 A O ATOM 1160 N LYS A 184 19.117 55.078 19.472 1.00 39.26 A N ATOM 1161 CA LYS A 184 18.493 54.887 18.173 1.00 39.63 A C ATOM 1162 CB LYS A 184 17.811 53.523 18.122 1.00 43.49 A C ATOM 1163 CG LYS A 184 17.448 53.067 16.724 1.00 47.35 A C ATOM 1164 CD LYS A 184 17.195 51.576 16.701 1.00 48.43 A C ATOM 1165 CE LYS A 184 16.731 51.137 15.336 1.00 49.12 A C ATOM 1166 NZ LYS A 184 15.467 51.830 14.980 1.00 56.98 A N ATOM 1167 C LYS A 184 17.513 55.998 17.764 1.00 42.01 A C ATOM 1168 O LYS A 184 16.767 56.506 18.598 1.00 43.68 A O ATOM 1169 N ASP A 185 17.539 56.358 16.473 1.00 41.05 A N ATOM 1170 CA ASP A 185 16.673 57.399 15.882 1.00 41.09 A C ATOM 1171 CB ASP A 185 15.186 57.015 15.962 1.00 40.56 A C ATOM 1172 CG ASP A 185 14.863 55.784 15.148 1.00 44.87 A C ATOM 1173 OD1 ASP A 185 15.342 55.696 13.988 1.00 40.39 A O ATOM 1174 OD2 ASP A 185 14.145 54.902 15.673 1.00 45.97 A O ATOM 1175 C ASP A 185 16.904 58.788 16.481 1.00 39.84 A C ATOM 1176 O ASP A 185 17.958 59.056 17.035 1.00 39.87 A O ATOM 1177 N GLY A 186 15.926 59.678 16.367 1.00 37.98 A N ATOM 1178 CA GLY A 186 16.124 61.037 16.856 1.00 42.09 A C ATOM 1179 C GLY A 186 17.271 61.730 16.122 1.00 35.32 A C ATOM 1180 O GLY A 186 17.203 61.888 14.908 1.00 34.38 A O ATOM 1181 N LEU A 187 18.310 62.133 16.858 1.00 35.14 A N ATOM 1182 CA LEU A 187 19.520 62.742 16.281 1.00 36.68 A C ATOM 1183 CB LEU A 187 20.445 63.270 17.384 1.00 33.87 A C ATOM 1184 CG LEU A 187 20.132 64.549 18.157 1.00 41.05 A C ATOM 1185 CD1 LEU A 187 18.816 64.428 18.889 1.00 41.96 A C ATOM 1186 CD2 LEU A 187 21.256 64.836 19.139 1.00 40.00 A C ATOM 1187 C LEU A 187 20.328 61.739 15.469 1.00 36.52 A C ATOM 1188 O LEU A 187 20.692 60.696 15.982 1.00 34.45 A O ATOM 1189 N LEU A 188 20.670 62.072 14.235 1.00 28.66 A N ATOM 1190 CA LEU A 188 21.407 61.123 13.408 1.00 32.72 A C ATOM 1191 CB LEU A 188 20.810 61.089 11.998 1.00 31.15 A C ATOM 1192 CG LEU A 188 19.303 60.853 11.947 1.00 31.13 A C ATOM 1193 CD1 LEU A 188 18.808 60.931 10.508 1.00 29.02 A C ATOM 1194 CD2 LEU A 188 18.978 59.509 12.566 1.00 31.96 A C ATOM 1195 C LEU A 188 22.911 61.416 13.335 1.00 31.76 A C ATOM 1196 O LEU A 188 23.711 60.546 12.980 1.00 30.80 A O ATOM 1197 N ALA A 189 23.284 62.644 13.671 1.00 31.31 A N ATOM 1198 CA ALA A 189 24.609 63.143 13.354 1.00 29.42 A C ATOM 1199 CB ALA A 189 24.900 62.920 11.862 1.00 25.40 A C ATOM 1200 C ALA A 189 24.666 64.626 13.656 1.00 30.99 A C ATOM 1201 O ALA A 189 23.631 65.277 13.807 1.00 30.84 A O ATOM 1202 N HIS A 190 25.879 65.164 13.744 1.00 30.53 A N ATOM 1203 CA HIS A 190 26.055 66.616 13.792 1.00 28.59 A C ATOM 1204 CB HIS A 190 25.875 67.173 15.198 1.00 30.59 A C ATOM 1205 CG HIS A 190 26.717 66.505 16.235 1.00 32.41 A C ATOM 1206 CD2 HIS A 190 27.950 65.943 16.167 1.00 32.40 A C ATOM 1207 ND1 HIS A 190 26.312 66.372 17.549 1.00 34.17 A N ATOM 1208 CE1 HIS A 190 27.249 65.754 18.239 1.00 35.39 A C ATOM 1209 NE2 HIS A 190 28.255 65.484 17.422 1.00 38.47 A N ATOM 1210 C HIS A 190 27.413 67.021 13.241 1.00 29.43 A C ATOM 1211 O HIS A 190 28.215 66.176 12.874 1.00 26.07 A O ATOM 1212 N ALA A 191 27.656 68.324 13.190 1.00 27.29 A N ATOM 1213 CA ALA A 191 28.872 68.833 12.583 1.00 33.76 A C ATOM 1214 CB ALA A 191 28.741 68.841 11.051 1.00 26.15 A C ATOM 1215 C ALA A 191 29.100 70.232 13.099 1.00 31.92 A C ATOM 1216 O ALA A 191 28.181 70.859 13.602 1.00 31.90 A O ATOM 1217 N PHE A 192 30.322 70.718 12.947 1.00 34.75 A N ATOM 1218 CA PHE A 192 30.723 72.020 13.464 1.00 35.03 A C ATOM 1219 CB PHE A 192 31.810 71.818 14.526 1.00 35.99 A C ATOM 1220 CG PHE A 192 31.422 70.836 15.602 1.00 37.81 A C ATOM 1221 CD1 PHE A 192 30.796 71.271 16.751 1.00 36.11 A C ATOM 1222 CD2 PHE A 192 31.662 69.478 15.445 1.00 37.79 A C ATOM 1223 CE1 PHE A 192 30.427 70.378 17.743 1.00 42.49 A C ATOM 1224 CE2 PHE A 192 31.294 68.575 16.440 1.00 41.71 A C ATOM 1225 CZ PHE A 192 30.677 69.030 17.592 1.00 38.38 A C ATOM 1226 C PHE A 192 31.231 72.932 12.339 1.00 33.66 A C ATOM 1227 O PHE A 192 31.881 72.458 11.398 1.00 29.02 A O ATOM 1228 N PRO A 193 30.978 74.251 12.463 1.00 30.26 A N ATOM 1229 CD PRO A 193 30.828 74.932 13.759 1.00 31.45 A C ATOM 1230 CA PRO A 193 31.310 75.190 11.386 1.00 30.62 A C ATOM 1231 CB PRO A 193 30.806 76.536 11.909 1.00 30.61 A C ATOM 1232 CG PRO A 193 30.451 76.323 13.367 1.00 35.13 A C ATOM 1233 C PRO A 193 32.821 75.251 11.211 1.00 34.13 A C ATOM 1234 O PRO A 193 33.540 74.881 12.141 1.00 33.25 A O ATOM 1235 N PRO A 194 33.295 75.723 10.042 1.00 34.93 A N ATOM 1236 CD PRO A 194 32.486 76.185 8.898 1.00 31.83 A C ATOM 1237 CA PRO A 194 34.743 75.788 9.778 1.00 34.90 A C ATOM 1238 CB PRO A 194 34.837 76.546 8.440 1.00 34.18 A C ATOM 1239 CG PRO A 194 33.510 76.306 7.764 1.00 34.91 A C ATOM 1240 C PRO A 194 35.514 76.531 10.869 1.00 33.19 A C ATOM 1241 O PRO A 194 34.982 77.436 11.504 1.00 32.78 A O ATOM 1242 N GLY A 195 36.771 76.149 11.067 1.00 36.64 A N ATOM 1243 CA GLY A 195 37.638 76.834 12.009 1.00 34.42 A C ATOM 1244 C GLY A 195 38.572 75.854 12.679 1.00 37.39 A C ATOM 1245 O GLY A 195 38.720 74.733 12.207 1.00 36.23 A O ATOM 1246 N PRO A 196 39.161 76.249 13.819 1.00 40.63 A N ATOM 1247 CD PRO A 196 38.708 77.374 14.648 1.00 40.98 A C ATOM 1248 CA PRO A 196 40.224 75.492 14.486 1.00 41.14 A C ATOM 1249 CB PRO A 196 40.818 76.518 15.472 1.00 36.71 A C ATOM 1250 CG PRO A 196 39.966 77.774 15.350 1.00 42.03 A C ATOM 1251 C PRO A 196 39.718 74.289 15.288 1.00 44.34 A C ATOM 1252 O PRO A 196 38.612 74.311 15.844 1.00 37.75 A O ATOM 1253 N GLY A 197 40.552 73.258 15.365 1.00 40.20 A N ATOM 1254 CA GLY A 197 40.311 72.148 16.265 1.00 41.00 A C ATOM 1255 C GLY A 197 39.137 71.304 15.845 1.00 43.02 A C ATOM 1256 O GLY A 197 39.163 70.694 14.787 1.00 40.75 A O ATOM 1257 N ILE A 198 38.102 71.271 16.678 1.00 35.00 A N ATOM 1258 CA ILE A 198 36.910 70.468 16.409 1.00 38.29 A C ATOM 1259 CB ILE A 198 36.073 70.271 17.705 1.00 41.03 A C ATOM 1260 CG2 ILE A 198 35.497 71.596 18.182 1.00 39.19 A C ATOM 1261 CG1 ILE A 198 34.965 69.234 17.509 1.00 41.77 A C ATOM 1262 CD1 ILE A 198 34.163 68.962 18.783 1.00 39.77 A C ATOM 1263 C ILE A 198 36.037 71.097 15.314 1.00 39.65 A C ATOM 1264 O ILE A 198 35.235 70.410 14.668 1.00 38.07 A O ATOM 1265 N GLN A 199 36.184 72.404 15.110 1.00 36.66 A N ATOM 1266 CA GLN A 199 35.414 73.082 14.074 1.00 35.66 A C ATOM 1267 CB GLN A 199 35.703 74.588 14.078 1.00 35.95 A C ATOM 1268 CG GLN A 199 35.240 75.223 15.388 1.00 37.86 A C ATOM 1269 CD GLN A 199 35.381 76.731 15.441 1.00 42.27 A C ATOM 1270 OE1 GLN A 199 35.661 77.293 16.504 1.00 43.34 A O ATOM 1271 NE2 GLN A 199 35.194 77.397 14.299 1.00 38.38 A N ATOM 1272 C GLN A 199 35.697 72.427 12.732 1.00 39.30 A C ATOM 1273 O GLN A 199 36.833 72.079 12.435 1.00 33.33 A O ATOM 1274 N GLY A 200 34.650 72.220 11.941 1.00 37.16 A N ATOM 1275 CA GLY A 200 34.785 71.482 10.700 1.00 33.38 A C ATOM 1276 C GLY A 200 34.449 70.003 10.841 1.00 35.39 A C ATOM 1277 O GLY A 200 34.203 69.322 9.845 1.00 32.60 A O ATOM 1278 N ASP A 201 34.438 69.490 12.069 1.00 32.26 A N ATOM 1279 CA ASP A 201 34.249 68.056 12.263 1.00 33.60 A C ATOM 1280 CB ASP A 201 34.710 67.623 13.664 1.00 36.95 A C ATOM 1281 CG ASP A 201 36.213 67.615 13.792 1.00 38.19 A C ATOM 1282 OD1 ASP A 201 36.881 67.931 12.779 1.00 38.79 A O ATOM 1283 OD2 ASP A 201 36.725 67.292 14.882 1.00 37.08 A O ATOM 1284 C ASP A 201 32.808 67.597 12.000 1.00 32.00 A C ATOM 1285 O ASP A 201 31.866 68.372 12.114 1.00 27.89 A O ATOM 1286 N ALA A 202 32.669 66.328 11.631 1.00 30.52 A N ATOM 1287 CA ALA A 202 31.382 65.723 11.342 1.00 30.73 A C ATOM 1288 CB ALA A 202 31.219 65.538 9.836 1.00 28.11 A C ATOM 1289 C ALA A 202 31.260 64.380 12.066 1.00 29.74 A C ATOM 1290 O ALA A 202 32.106 63.495 11.905 1.00 30.45 A O ATOM 1291 N HIS A 203 30.217 64.237 12.872 1.00 28.51 A N ATOM 1292 CA HIS A 203 30.030 63.019 13.668 1.00 32.05 A C ATOM 1293 CB HIS A 203 29.989 63.342 15.161 1.00 30.75 A C ATOM 1294 CG HIS A 203 31.246 63.978 15.686 1.00 36.71 A C ATOM 1295 CD2 HIS A 203 32.525 63.552 15.681 1.00 40.23 A C ATOM 1296 ND1 HIS A 203 31.241 65.212 16.307 1.00 43.80 A N ATOM 1297 CE1 HIS A 203 32.471 65.510 16.682 1.00 40.13 A C ATOM 1298 NE2 HIS A 203 33.271 64.532 16.321 1.00 40.75 A N ATOM 1299 C HIS A 203 28.738 62.303 13.275 1.00 30.16 A C ATOM 1300 O HIS A 203 27.707 62.942 13.094 1.00 27.41 A O ATOM 1301 N PHE A 204 28.808 60.983 13.136 1.00 30.15 A N ATOM 1302 CA PHE A 204 27.643 60.176 12.776 1.00 32.11 A C ATOM 1303 CB PHE A 204 27.902 59.437 11.465 1.00 29.08 A C ATOM 1304 CG PHE A 204 28.249 60.354 10.335 1.00 31.22 A C ATOM 1305 CD1 PHE A 204 29.556 60.771 10.143 1.00 28.93 A C ATOM 1306 CD2 PHE A 204 27.258 60.838 9.491 1.00 31.83 A C ATOM 1307 CE1 PHE A 204 29.877 61.643 9.096 1.00 32.83 A C ATOM 1308 CE2 PHE A 204 27.566 61.705 8.450 1.00 26.40 A C ATOM 1309 CZ PHE A 204 28.878 62.107 8.257 1.00 28.70 A C ATOM 1310 C PHE A 204 27.270 59.191 13.881 1.00 32.72 A C ATOM 1311 O PHE A 204 28.121 58.447 14.375 1.00 30.18 A O ATOM 1312 N ASP A 205 25.995 59.193 14.264 1.00 32.89 A N ATOM 1313 CA ASP A 205 25.531 58.348 15.361 1.00 31.25 A C ATOM 1314 CB ASP A 205 24.166 58.813 15.873 1.00 34.66 A C ATOM 1315 CG ASP A 205 23.764 58.124 17.183 1.00 35.48 A C ATOM 1316 OD1 ASP A 205 24.413 57.140 17.591 1.00 33.68 A O ATOM 1317 OD2 ASP A 205 22.798 58.576 17.811 1.00 36.15 A O ATOM 1318 C ASP A 205 25.447 56.890 14.942 1.00 33.25 A C ATOM 1319 O ASP A 205 24.564 56.509 14.165 1.00 35.40 A O ATOM 1320 N ASP A 206 26.354 56.075 15.472 1.00 32.88 A N ATOM 1321 CA ASP A 206 26.460 54.679 15.067 1.00 32.84 A C ATOM 1322 CB ASP A 206 27.881 54.164 15.316 1.00 35.80 A C ATOM 1323 CG ASP A 206 28.316 53.090 14.313 1.00 32.37 A C ATOM 1324 OD1 ASP A 206 27.515 52.677 13.449 1.00 30.53 A O ATOM 1325 OD2 ASP A 206 29.479 52.649 14.400 1.00 38.85 A O ATOM 1326 C ASP A 206 25.410 53.804 15.775 1.00 34.93 A C ATOM 1327 O ASP A 206 25.379 52.598 15.604 1.00 32.58 A O ATOM 1328 N ASP A 207 24.535 54.417 16.565 1.00 36.15 A N ATOM 1329 CA ASP A 207 23.377 53.679 17.058 1.00 37.65 A C ATOM 1330 CB ASP A 207 22.838 54.274 18.363 1.00 40.05 A C ATOM 1331 CG ASP A 207 23.551 53.721 19.582 1.00 40.19 A C ATOM 1332 OD1 ASP A 207 24.125 52.614 19.464 1.00 34.03 A O ATOM 1333 OD2 ASP A 207 23.543 54.397 20.631 1.00 32.45 A O ATOM 1334 C ASP A 207 22.297 53.647 15.990 1.00 37.28 A C ATOM 1335 O ASP A 207 21.233 53.068 16.189 1.00 39.64 A O ATOM 1336 N GLU A 208 22.567 54.290 14.860 1.00 36.27 A N ATOM 1337 CA GLU A 208 21.682 54.189 13.708 1.00 34.34 A C ATOM 1338 CB GLU A 208 21.610 55.510 12.940 1.00 35.14 A C ATOM 1339 CG GLU A 208 21.270 56.703 13.783 1.00 36.32 A C ATOM 1340 CD GLU A 208 19.932 56.568 14.456 1.00 38.56 A C ATOM 1341 OE1 GLU A 208 19.158 55.646 14.103 1.00 39.58 A O ATOM 1342 OE2 GLU A 208 19.651 57.395 15.343 1.00 40.48 A O ATOM 1343 C GLU A 208 22.224 53.132 12.773 1.00 36.27 A C ATOM 1344 O GLU A 208 23.437 52.873 12.737 1.00 36.67 A O ATOM 1345 N LEU A 209 21.315 52.536 12.012 1.00 33.12 A N ATOM 1346 CA LEU A 209 21.673 51.624 10.955 1.00 33.68 A C ATOM 1347 CB LEU A 209 20.518 50.678 10.624 1.00 32.96 A C ATOM 1348 CG LEU A 209 20.799 49.669 9.504 1.00 33.74 A C ATOM 1349 CD1 LEU A 209 21.829 48.648 9.982 1.00 32.63 A C ATOM 1350 CD2 LEU A 209 19.513 48.984 9.030 1.00 35.24 A C ATOM 1351 C LEU A 209 21.990 52.467 9.729 1.00 36.11 A C ATOM 1352 O LEU A 209 21.096 53.110 9.168 1.00 35.91 A O ATOM 1353 N TRP A 210 23.259 52.463 9.332 1.00 32.31 A N ATOM 1354 CA TRP A 210 23.708 53.173 8.150 1.00 30.84 A C ATOM 1355 CB TRP A 210 25.118 53.736 8.369 1.00 26.95 A C ATOM 1356 CG TRP A 210 25.091 54.779 9.437 1.00 29.29 A C ATOM 1357 CD2 TRP A 210 24.482 56.069 9.345 1.00 28.67 A C ATOM 1358 CE2 TRP A 210 24.648 56.700 10.592 1.00 29.44 A C ATOM 1359 CE3 TRP A 210 23.831 56.766 8.316 1.00 28.89 A C ATOM 1360 CD1 TRP A 210 25.562 54.667 10.711 1.00 32.64 A C ATOM 1361 NE1 TRP A 210 25.310 55.822 11.412 1.00 31.23 A N ATOM 1362 CZ2 TRP A 210 24.175 57.989 10.846 1.00 29.34 A C ATOM 1363 CZ3 TRP A 210 23.374 58.046 8.567 1.00 28.07 A C ATOM 1364 CH2 TRP A 210 23.547 58.644 9.821 1.00 28.71 A C ATOM 1365 C TRP A 210 23.641 52.282 6.922 1.00 36.87 A C ATOM 1366 O TRP A 210 24.022 51.107 6.956 1.00 34.27 A O ATOM 1367 N SER A 211 23.125 52.851 5.842 1.00 31.60 A N ATOM 1368 CA SER A 211 23.035 52.144 4.591 1.00 31.47 A C ATOM 1369 CB SER A 211 21.718 51.360 4.503 1.00 32.96 A C ATOM 1370 OG SER A 211 20.583 52.223 4.556 1.00 32.66 A O ATOM 1371 C SER A 211 23.072 53.216 3.524 1.00 30.24 A C ATOM 1372 O SER A 211 23.582 54.320 3.741 1.00 28.81 A O ATOM 1373 N LEU A 212 22.493 52.910 2.378 1.00 29.74 A N ATOM 1374 CA LEU A 212 22.322 53.944 1.381 1.00 34.63 A C ATOM 1375 CB LEU A 212 22.904 53.507 0.042 1.00 30.11 A C ATOM 1376 CG LEU A 212 24.425 53.362 0.170 1.00 29.06 A C ATOM 1377 CD1 LEU A 212 25.139 53.214 −1.191 1.00 34.37 A C ATOM 1378 CD2 LEU A 212 25.018 54.547 0.926 1.00 29.64 A C ATOM 1379 C LEU A 212 20.855 54.413 1.325 1.00 37.49 A C ATOM 1380 O LEU A 212 20.390 54.952 0.314 1.00 34.59 A O ATOM 1381 N GLY A 213 20.148 54.215 2.444 1.00 34.07 A N ATOM 1382 CA GLY A 213 18.811 54.763 2.631 1.00 34.89 A C ATOM 1383 C GLY A 213 17.730 53.901 2.003 1.00 40.31 A C ATOM 1384 O GLY A 213 16.537 54.058 2.282 1.00 39.26 A O ATOM 1385 N LYS A 389 18.161 52.976 1.142 1.00 40.84 A N ATOM 1386 CA LYS A 389 17.224 52.070 0.484 1.00 44.47 A C ATOM 1387 CB LYS A 389 17.739 51.721 −0.902 1.00 47.97 A C ATOM 1388 CG LYS A 389 16.731 51.032 −1.767 1.00 54.22 A C ATOM 1389 CD LYS A 389 16.228 51.966 −2.865 1.00 59.73 A C ATOM 1390 CE LYS A 389 15.956 51.187 −4.174 1.00 64.08 A C ATOM 1391 NZ LYS A 389 17.244 50.652 −4.770 1.00 59.91 A N ATOM 1392 C LYS A 389 17.014 50.781 1.279 1.00 46.09 A C ATOM 1393 O LYS A 389 17.956 50.226 1.848 1.00 42.92 A O ATOM 1394 N GLY A 390 15.774 50.304 1.312 1.00 43.18 A N ATOM 1395 CA GLY A 390 15.463 49.050 1.968 1.00 41.35 A C ATOM 1396 C GLY A 390 15.269 49.252 3.455 1.00 44.81 A C ATOM 1397 O GLY A 390 14.147 49.200 3.958 1.00 48.67 A O ATOM 1398 N GLN A 391 16.371 49.461 4.158 1.00 37.85 A N ATOM 1399 CA GLN A 391 16.341 49.789 5.573 1.00 39.08 A C ATOM 1400 CB GLN A 391 16.397 48.521 6.429 1.00 40.91 A C ATOM 1401 CG GLN A 391 15.207 47.580 6.249 1.00 49.33 A C ATOM 1402 CD GLN A 391 15.457 46.198 6.831 1.00 43.68 A C ATOM 1403 OE1 GLN A 391 16.067 46.056 7.896 1.00 41.17 A O ATOM 1404 NE2 GLN A 391 14.997 45.168 6.122 1.00 43.13 A N ATOM 1405 C GLN A 391 17.556 50.668 5.862 1.00 40.87 A C ATOM 1406 O GLN A 391 18.532 50.671 5.088 1.00 35.63 A O ATOM 1407 N GLY A 392 17.486 51.425 6.957 1.00 35.12 A N ATOM 1408 CA GLY A 392 18.602 52.239 7.397 1.00 36.35 A C ATOM 1409 C GLY A 392 18.623 53.646 6.833 1.00 34.96 A C ATOM 1410 O GLY A 392 17.931 53.953 5.859 1.00 32.84 A O ATOM 1411 N TYR A 393 19.418 54.509 7.455 1.00 32.10 A N ATOM 1412 CA TYR A 393 19.563 55.890 6.994 1.00 33.29 A C ATOM 1413 CB TYR A 393 19.867 56.808 8.170 1.00 29.08 A C ATOM 1414 CG TYR A 393 18.738 56.908 9.161 1.00 33.18 A C ATOM 1415 CD1 TYR A 393 17.586 57.637 8.863 1.00 31.83 A C ATOM 1416 CE1 TYR A 393 16.549 57.739 9.779 1.00 32.42 A C ATOM 1417 CD2 TYR A 393 18.822 56.276 10.404 1.00 34.63 A C ATOM 1418 CE2 TYR A 393 17.797 56.365 11.320 1.00 33.36 A C ATOM 1419 CZ TYR A 393 16.667 57.100 11.008 1.00 37.24 A C ATOM 1420 OH TYR A 393 15.660 57.179 11.936 1.00 36.80 A O ATOM 1421 C TYR A 393 20.673 56.022 5.955 1.00 31.36 A C ATOM 1422 O TYR A 393 21.725 55.421 6.108 1.00 30.35 A O ATOM 1423 N SER A 394 20.438 56.812 4.908 1.00 29.12 A N ATOM 1424 CA SER A 394 21.460 57.022 3.886 1.00 27.20 A C ATOM 1425 CB SER A 394 20.888 57.760 2.674 1.00 28.20 A C ATOM 1426 OG SER A 394 21.922 58.127 1.783 1.00 29.11 A O ATOM 1427 C SER A 394 22.660 57.785 4.435 1.00 28.00 A C ATOM 1428 O SER A 394 22.564 58.969 4.764 1.00 24.83 A O ATOM 1429 N LEU A 395 23.796 57.102 4.522 1.00 27.18 A N ATOM 1430 CA LEU A 395 25.033 57.746 4.936 1.00 25.19 A C ATOM 1431 CB LEU A 395 26.172 56.724 4.972 1.00 26.89 A C ATOM 1432 CG LEU A 395 27.475 57.319 5.494 1.00 28.46 A C ATOM 1433 CD1 LEU A 395 27.228 57.961 6.845 1.00 28.96 A C ATOM 1434 CD2 LEU A 395 28.583 56.271 5.562 1.00 27.24 A C ATOM 1435 C LEU A 395 25.396 58.861 3.963 1.00 28.02 A C ATOM 1436 O LEU A 395 25.913 59.910 4.356 1.00 25.06 A O ATOM 1437 N PHE A 396 25.146 58.612 2.683 1.00 24.74 A N ATOM 1438 CA PHE A 396 25.446 59.580 1.643 1.00 25.16 A C ATOM 1439 CB PHE A 396 25.053 59.004 0.272 1.00 27.27 A C ATOM 1440 CG PHE A 396 25.060 60.014 −0.849 1.00 25.95 A C ATOM 1441 CD1 PHE A 396 26.192 60.782 −1.118 1.00 26.93 A C ATOM 1442 CD2 PHE A 396 23.949 60.170 −1.659 1.00 26.43 A C ATOM 1443 CE1 PHE A 396 26.191 61.712 −2.159 1.00 24.65 A C ATOM 1444 CE2 PHE A 396 23.948 61.088 −2.713 1.00 28.53 A C ATOM 1445 CZ PHE A 396 25.059 61.862 −2.953 1.00 24.03 A C ATOM 1446 C PHE A 396 24.710 60.886 1.932 1.00 23.05 A C ATOM 1447 O PHE A 396 25.322 61.921 2.163 1.00 24.92 A O ATOM 1448 N LEU A 397 23.391 60.818 1.952 1.00 24.15 A N ATOM 1449 CA LEU A 397 22.566 61.990 2.200 1.00 23.87 A C ATOM 1450 CB LEU A 397 21.091 61.593 2.167 1.00 20.75 A C ATOM 1451 CG LEU A 397 20.513 61.106 0.833 1.00 23.49 A C ATOM 1452 CD1 LEU A 397 19.095 60.582 0.995 1.00 24.16 A C ATOM 1453 CD2 LEU A 397 20.545 62.210 −0.236 1.00 25.17 A C ATOM 1454 C LEU A 397 22.919 62.698 3.521 1.00 22.52 A C ATOM 1455 O LEU A 397 23.093 63.908 3.552 1.00 22.15 A O ATOM 1456 N VAL A 398 23.024 61.953 4.616 1.00 21.47 A N ATOM 1457 CA VAL A 398 23.282 62.584 5.916 1.00 21.80 A C ATOM 1458 CB VAL A 398 23.221 61.553 7.070 1.00 26.16 A C ATOM 1459 CG1 VAL A 398 23.678 62.173 8.373 1.00 23.35 A C ATOM 1460 CG2 VAL A 398 21.801 61.001 7.205 1.00 22.85 A C ATOM 1461 C VAL A 398 24.632 63.306 5.906 1.00 26.58 A C ATOM 1462 O VAL A 398 24.776 64.411 6.454 1.00 24.30 A O ATOM 1463 N ALA A 399 25.610 62.673 5.262 1.00 21.81 A N ATOM 1464 CA ALA A 399 26.953 63.227 5.168 1.00 27.72 A C ATOM 1465 CB ALA A 399 27.942 62.169 4.645 1.00 25.02 A C ATOM 1466 C ALA A 399 26.975 64.493 4.297 1.00 24.20 A C ATOM 1467 O ALA A 399 27.600 65.494 4.647 1.00 23.61 A O ATOM 1468 N ALA A 400 26.265 64.448 3.180 1.00 21.18 A N ATOM 1469 CA ALA A 400 26.159 65.621 2.312 1.00 25.85 A C ATOM 1470 CB ALA A 400 25.225 65.328 1.145 1.00 22.45 A C ATOM 1471 C ALA A 400 25.656 66.812 3.123 1.00 25.78 A C ATOM 1472 O ALA A 400 26.181 67.933 3.036 1.00 25.57 A O ATOM 1473 N HIS A 401 24.643 66.546 3.939 1.00 25.02 A N ATOM 1474 CA HIS A 401 24.037 67.572 4.777 1.00 21.15 A C ATOM 1475 CB HIS A 401 22.731 67.031 5.373 1.00 21.64 A C ATOM 1476 CG HIS A 401 22.119 67.921 6.401 1.00 21.81 A C ATOM 1477 CD2 HIS A 401 22.501 68.212 7.667 1.00 22.60 A C ATOM 1478 ND1 HIS A 401 20.988 68.665 6.161 1.00 21.74 A N ATOM 1479 CE1 HIS A 401 20.695 69.380 7.231 1.00 20.89 A C ATOM 1480 NE2 HIS A 401 21.591 69.116 8.163 1.00 21.45 A N ATOM 1481 C HIS A 401 25.002 68.077 5.866 1.00 22.61 A C ATOM 1482 O HIS A 401 25.174 69.281 6.035 1.00 20.12 A O ATOM 1483 N GLU A 402 25.624 67.156 6.599 1.00 20.74 A N ATOM 1484 CA GLU A 402 26.581 67.524 7.635 1.00 23.20 A C ATOM 1485 CB GLU A 402 27.007 66.289 8.431 1.00 22.77 A C ATOM 1486 CG GLU A 402 25.821 65.520 9.031 1.00 25.19 A C ATOM 1487 CD GLU A 402 25.074 66.302 10.100 1.00 24.15 A C ATOM 1488 OE1 GLU A 402 25.638 67.273 10.638 1.00 25.08 A O ATOM 1489 OE2 GLU A 402 23.915 65.934 10.409 1.00 26.52 A O ATOM 1490 C GLU A 402 27.818 68.277 7.100 1.00 22.76 A C ATOM 1491 O GLU A 402 28.285 69.229 7.725 1.00 22.99 A O ATOM 1492 N PHE A 403 28.341 67.846 5.953 1.00 24.34 A N ATOM 1493 CA PHE A 403 29.439 68.566 5.282 1.00 25.52 A C ATOM 1494 CB PHE A 403 29.884 67.830 4.015 1.00 24.24 A C ATOM 1495 CG PHE A 403 30.441 66.457 4.275 1.00 25.85 A C ATOM 1496 CD1 PHE A 403 30.769 66.058 5.557 1.00 25.75 A C ATOM 1497 CD2 PHE A 403 30.657 65.573 3.226 1.00 26.81 A C ATOM 1498 CE1 PHE A 403 31.283 64.796 5.800 1.00 27.96 A C ATOM 1499 CE2 PHE A 403 31.175 64.320 3.452 1.00 26.04 A C ATOM 1500 CZ PHE A 403 31.487 63.926 4.752 1.00 27.42 A C ATOM 1501 C PHE A 403 29.045 70.010 4.948 1.00 26.65 A C ATOM 1502 O PHE A 403 29.883 70.917 4.970 1.00 28.46 A O ATOM 1503 N GLY A 404 27.762 70.213 4.646 1.00 25.27 A N ATOM 1504 CA GLY A 404 27.202 71.549 4.490 1.00 24.54 A C ATOM 1505 C GLY A 404 27.475 72.444 5.687 1.00 26.29 A C ATOM 1506 O GLY A 404 27.891 73.599 5.540 1.00 25.47 A O ATOM 1507 N HIS A 405 27.237 71.917 6.886 1.00 27.24 A N ATOM 1508 CA HIS A 405 27.625 72.627 8.107 1.00 24.18 A C ATOM 1509 CB HIS A 405 27.174 71.845 9.341 1.00 25.29 A C ATOM 1510 CG HIS A 405 25.687 71.821 9.520 1.00 21.70 A C ATOM 1511 CD2 HIS A 405 24.838 70.783 9.748 1.00 22.91 A C ATOM 1512 ND1 HIS A 405 24.920 72.952 9.469 1.00 21.35 A N ATOM 1513 CE1 HIS A 405 23.641 72.627 9.676 1.00 26.04 A C ATOM 1514 NE2 HIS A 405 23.579 71.323 9.844 1.00 26.12 A N ATOM 1515 C HIS A 405 29.143 72.868 8.170 1.00 26.84 A C ATOM 1516 O HIS A 405 29.593 73.952 8.565 1.00 26.69 A O ATOM 1517 N ALA A 406 29.914 71.843 7.807 1.00 24.57 A N ATOM 1518 CA ALA A 406 31.375 71.881 7.873 1.00 26.21 A C ATOM 1519 CB ALA A 406 31.988 70.473 7.560 1.00 21.40 A C ATOM 1520 C ALA A 406 31.964 72.939 6.934 1.00 29.85 A C ATOM 1521 O ALA A 406 33.139 73.296 7.049 1.00 32.04 A O ATOM 1522 N LEU A 407 31.147 73.414 5.997 1.00 26.50 A N ATOM 1523 CA LEU A 407 31.556 74.462 5.080 1.00 29.86 A C ATOM 1524 CB LEU A 407 31.084 74.156 3.656 1.00 24.34 A C ATOM 1525 CG LEU A 407 31.689 72.909 3.021 1.00 26.87 A C ATOM 1526 CD1 LEU A 407 31.108 72.738 1.639 1.00 28.31 A C ATOM 1527 CD2 LEU A 407 33.238 72.993 2.978 1.00 24.97 A C ATOM 1528 C LEU A 407 30.988 75.791 5.537 1.00 28.40 A C ATOM 1529 O LEU A 407 31.241 76.826 4.915 1.00 28.98 A O ATOM 1530 N GLY A 408 30.200 75.753 6.609 1.00 29.31 A N ATOM 1531 CA GLY A 408 29.607 76.955 7.177 1.00 25.53 A C ATOM 1532 C GLY A 408 28.114 77.196 6.946 1.00 28.25 A C ATOM 1533 O GLY A 408 27.613 78.277 7.255 1.00 29.02 A O ATOM 1534 N LEU A 409 27.383 76.215 6.423 1.00 27.35 A N ATOM 1535 CA LEU A 409 25.939 76.420 6.204 1.00 25.94 A C ATOM 1536 CB LEU A 409 25.417 75.563 5.054 1.00 23.12 A C ATOM 1537 CG LEU A 409 25.981 75.808 3.648 1.00 28.27 A C ATOM 1538 CD1 LEU A 409 25.372 74.827 2.654 1.00 24.95 A C ATOM 1539 CD2 LEU A 409 25.733 77.239 3.195 1.00 23.70 A C ATOM 1540 C LEU A 409 25.096 76.156 7.451 1.00 27.11 A C ATOM 1541 O LEU A 409 25.404 75.267 8.232 1.00 30.58 A O ATOM 1542 N ASP A 410 24.032 76.941 7.624 1.00 28.33 A N ATOM 1543 CA ASP A 410 23.008 76.693 8.641 1.00 31.06 A C ATOM 1544 CB ASP A 410 22.412 78.001 9.162 1.00 27.79 A C ATOM 1545 CG ASP A 410 23.432 78.886 9.802 1.00 35.16 A C ATOM 1546 OD1 ASP A 410 24.254 78.365 10.584 1.00 32.76 A O ATOM 1547 OD2 ASP A 410 23.410 80.102 9.527 1.00 40.03 A O ATOM 1548 C ASP A 410 21.870 75.923 8.020 1.00 29.46 A C ATOM 1549 O ASP A 410 21.859 75.676 6.831 1.00 26.28 A O ATOM 1550 N HIS A 411 20.874 75.588 8.833 1.00 30.88 A N ATOM 1551 CA HIS A 411 19.693 74.895 8.332 1.00 25.74 A C ATOM 1552 CB HIS A 411 18.847 74.328 9.488 1.00 26.57 A C ATOM 1553 CG HIS A 411 19.465 73.136 10.152 1.00 27.70 A C ATOM 1554 CD2 HIS A 411 20.207 72.121 9.639 1.00 24.94 A C ATOM 1555 ND1 HIS A 411 19.389 72.915 11.508 1.00 27.71 A N ATOM 1556 CE1 HIS A 411 20.043 71.804 11.806 1.00 26.48 A C ATOM 1557 NE2 HIS A 411 20.552 71.311 10.702 1.00 25.41 A N ATOM 1558 C HIS A 411 18.846 75.784 7.452 1.00 25.02 A C ATOM 1559 O HIS A 411 18.787 76.986 7.630 1.00 28.01 A O ATOM 1560 N SER A 412 18.182 75.154 6.498 1.00 27.13 A N ATOM 1561 CA SER A 412 17.218 75.810 5.638 1.00 24.71 A C ATOM 1562 CB SER A 412 17.278 75.186 4.256 1.00 23.48 A C ATOM 1563 OG SER A 412 16.358 75.826 3.395 1.00 25.12 A O ATOM 1564 C SER A 412 15.825 75.559 6.187 1.00 27.53 A C ATOM 1565 O SER A 412 15.589 74.550 6.843 1.00 23.98 A O ATOM 1566 N SER A 413 14.902 76.463 5.873 1.00 27.76 A N ATOM 1567 CA SER A 413 13.498 76.285 6.204 1.00 25.64 A C ATOM 1568 CB SER A 413 12.921 77.595 6.736 1.00 30.17 A C ATOM 1569 OG SER A 413 12.916 78.582 5.723 1.00 37.76 A O ATOM 1570 C SER A 413 12.687 75.761 5.000 1.00 30.25 A C ATOM 1571 O SER A 413 11.485 75.493 5.093 1.00 32.18 A O ATOM 1572 N VAL A 414 13.358 75.602 3.870 1.00 26.90 A N ATOM 1573 CA VAL A 414 12.789 74.910 2.722 1.00 28.51 A C ATOM 1574 CB VAL A 414 13.613 75.215 1.454 1.00 27.08 A C ATOM 1575 CG1 VAL A 414 13.077 74.433 0.260 1.00 27.63 A C ATOM 1576 CG2 VAL A 414 13.603 76.705 1.189 1.00 27.48 A C ATOM 1577 C VAL A 414 12.860 73.417 2.985 1.00 29.36 A C ATOM 1578 O VAL A 414 13.954 72.865 3.062 1.00 27.70 A O ATOM 1579 N PRO A 415 11.698 72.750 3.115 1.00 29.12 A N ATOM 1580 CD PRO A 415 10.352 73.314 2.937 1.00 29.93 A C ATOM 1581 CA PRO A 415 11.656 71.326 3.487 1.00 30.94 A C ATOM 1582 CB PRO A 415 10.139 71.032 3.615 1.00 30.46 A C ATOM 1583 CG PRO A 415 9.482 72.375 3.767 1.00 27.58 A C ATOM 1584 C PRO A 415 12.313 70.370 2.465 1.00 31.71 A C ATOM 1585 O PRO A 415 12.746 69.275 2.832 1.00 32.24 A O ATOM 1586 N GLU A 416 12.366 70.771 1.197 1.00 31.03 A N ATOM 1587 CA GLU A 416 12.990 69.957 0.156 1.00 31.86 A C ATOM 1588 CB GLU A 416 12.451 70.353 −1.218 1.00 32.73 A C ATOM 1589 CG GLU A 416 10.947 70.201 −1.375 1.00 38.14 A C ATOM 1590 CD GLU A 416 10.172 71.362 −0.756 1.00 34.62 A C ATOM 1591 OE1 GLU A 416 10.652 72.523 −0.824 1.00 33.64 A O ATOM 1592 OE2 GLU A 416 9.070 71.107 −0.225 1.00 36.74 A O ATOM 1593 C GLU A 416 14.516 70.083 0.126 1.00 31.87 A C ATOM 1594 O GLU A 416 15.216 69.209 −0.407 1.00 31.00 A O ATOM 1595 N ALA A 417 15.023 71.181 0.681 1.00 27.80 A N ATOM 1596 CA ALA A 417 16.448 71.475 0.615 1.00 30.80 A C ATOM 1597 CB ALA A 417 16.729 72.872 1.186 1.00 25.54 A C ATOM 1598 C ALA A 417 17.281 70.431 1.346 1.00 26.62 A C ATOM 1599 O ALA A 417 16.853 69.886 2.367 1.00 27.97 A O ATOM 1600 N LEU A 418 18.489 70.177 0.836 1.00 29.44 A N ATOM 1601 CA LEU A 418 19.444 69.339 1.553 1.00 27.09 A C ATOM 1602 CB LEU A 418 20.784 69.241 0.795 1.00 23.23 A C ATOM 1603 CG LEU A 418 21.898 68.451 1.496 1.00 22.75 A C ATOM 1604 CD1 LEU A 418 21.472 67.022 1.759 1.00 24.61 A C ATOM 1605 CD2 LEU A 418 23.237 68.457 0.725 1.00 24.14 A C ATOM 1606 C LEU A 418 19.677 69.820 2.998 1.00 23.84 A C ATOM 1607 O LEU A 418 19.852 69.003 3.902 1.00 23.01 A O ATOM 1608 N MET A 419 19.717 71.137 3.215 1.00 26.13 A N ATOM 1609 CA MET A 419 20.058 71.671 4.542 1.00 22.55 A C ATOM 1610 CB MET A 419 20.798 73.007 4.445 1.00 19.43 A C ATOM 1611 CG MET A 419 22.178 72.936 3.778 1.00 21.30 A C ATOM 1612 SD MET A 419 23.209 71.597 4.408 1.00 21.22 A S ATOM 1613 CE MET A 419 23.484 72.101 6.120 1.00 23.60 A C ATOM 1614 C MET A 419 18.855 71.782 5.506 1.00 24.87 A C ATOM 1615 O MET A 419 18.979 72.296 6.622 1.00 23.86 A O ATOM 1616 N TYR A 420 17.695 71.317 5.074 1.00 25.66 A N ATOM 1617 CA TYR A 420 16.569 71.175 5.988 1.00 26.26 A C ATOM 1618 CB TYR A 420 15.358 70.652 5.227 1.00 24.51 A C ATOM 1619 CG TYR A 420 14.034 70.775 5.957 1.00 28.59 A C ATOM 1620 CD1 TYR A 420 13.454 72.020 6.204 1.00 26.59 A C ATOM 1621 CE1 TYR A 420 12.221 72.123 6.866 1.00 29.27 A C ATOM 1622 CD2 TYR A 420 13.338 69.637 6.359 1.00 27.63 A C ATOM 1623 CE2 TYR A 420 12.116 69.731 7.007 1.00 28.55 A C ATOM 1624 CZ TYR A 420 11.562 70.966 7.253 1.00 28.01 A C ATOM 1625 OH TYR A 420 10.348 71.030 7.894 1.00 33.11 A O ATOM 1626 C TYR A 420 16.993 70.194 7.085 1.00 26.07 A C ATOM 1627 O TYR A 420 17.688 69.228 6.815 1.00 25.89 A O ATOM 1628 N PRO A 421 16.572 70.437 8.330 1.00 29.40 A N ATOM 1629 CD PRO A 421 15.558 71.423 8.712 1.00 26.73 A C ATOM 1630 CA PRO A 421 17.047 69.657 9.482 1.00 26.14 A C ATOM 1631 CB PRO A 421 16.450 70.395 10.679 1.00 26.98 A C ATOM 1632 CG PRO A 421 15.867 71.644 10.134 1.00 27.02 A C ATOM 1633 C PRO A 421 16.572 68.205 2.486 1.00 24.25 A C ATOM 1634 O PRO A 421 17.323 67.336 9.907 1.00 26.40 A O ATOM 1635 N MET A 422 15.354 67.945 9.022 1.00 25.97 A N ATOM 1636 CA MET A 422 14.784 66.589 9.059 1.00 29.90 A C ATOM 1637 CB MET A 422 13.271 66.615 8.855 1.00 25.47 A C ATOM 1638 CG MET A 422 12.493 67.323 9.947 1.00 31.29 A C ATOM 1639 SD MET A 422 10.704 67.261 9.632 1.00 35.01 A S ATOM 1640 CE MET A 422 10.208 68.638 10.667 1.00 25.43 A C ATOM 1641 C MET A 422 15.387 65.680 7.997 1.00 32.93 A C ATOM 1642 O MET A 422 15.669 66.122 6.887 1.00 25.94 A O ATOM 1643 N TYR A 423 15.567 64.410 8.351 1.00 31.03 A N ATOM 1644 CA TYR A 423 15.959 63.393 7.391 1.00 28.30 A C ATOM 1645 CB TYR A 423 16.388 62.101 8.105 1.00 29.27 A C ATOM 1646 CG TYR A 423 16.748 61.005 7.128 1.00 32.33 A C ATOM 1647 CD1 TYR A 423 15.805 60.062 6.726 1.00 33.00 A C ATOM 1648 CE1 TYR A 423 16.129 59.072 5.812 1.00 32.64 A C ATOM 1649 CD2 TYR A 423 18.018 60.940 6.567 1.00 31.17 A C ATOM 1650 CE2 TYR A 423 18.350 59.949 5.652 1.00 29.46 A C ATOM 1651 CZ TYR A 423 17.401 59.026 5.271 1.00 30.29 A C ATOM 1652 OH TYR A 423 17.725 58.046 4.351 1.00 29.62 A O ATOM 1653 C TYR A 423 14.787 63.092 6.458 1.00 32.43 A C ATOM 1654 O TYR A 423 13.672 62.824 6.912 1.00 32.50 A O ATOM 1655 N ARG A 424 15.038 63.146 5.159 1.00 30.14 A N ATOM 1656 CA ARG A 424 14.054 62.721 4.177 1.00 34.92 A C ATOM 1657 CB ARG A 424 13.285 63.915 3.595 1.00 36.59 A C ATOM 1658 CG ARG A 424 14.093 64.733 2.590 1.00 41.10 A C ATOM 1659 CD ARG A 424 13.209 65.336 1.496 1.00 46.52 A C ATOM 1660 NE ARG A 424 14.014 65.973 0.460 1.00 40.47 A N ATOM 1661 CZ ARG A 424 13.712 65.984 −0.836 1.00 43.48 A C ATOM 1662 NH1 ARG A 424 12.609 65.386 −1.276 1.00 48.17 A N ATOM 1663 NH2 ARG A 424 14.524 66.585 −1.698 1.00 37.23 A N ATOM 1664 C ARG A 424 14.791 61.993 3.066 1.00 34.15 A C ATOM 1665 O ARG A 424 15.629 62.583 2.378 1.00 36.98 A O ATOM 1666 N PHE A 425 14.509 60.707 2.893 1.00 33.04 A N ATOM 1667 CA PHE A 425 15.196 59.949 1.857 1.00 32.72 A C ATOM 1668 CB PHE A 425 14.980 58.445 1.990 1.00 34.73 A C ATOM 1669 CG PHE A 425 15.611 57.657 0.876 1.00 32.87 A C ATOM 1670 CD1 PHE A 425 16.973 57.428 0.862 1.00 32.99 A C ATOM 1671 CD2 PHE A 425 14.852 57.185 −0.175 1.00 33.53 A C ATOM 1672 CE1 PHE A 425 17.567 56.717 −0.174 1.00 34.01 A C ATOM 1673 CE2 PHE A 425 15.441 56.475 −1.214 1.00 35.94 A C ATOM 1674 CZ PHE A 425 16.797 56.238 −1.207 1.00 33.62 A C ATOM 1675 C PHE A 425 14.730 60.394 0.489 1.00 31.38 A C ATOM 1676 O PHE A 425 13.567 60.707 0.297 1.00 31.98 A O ATOM 1677 N THR A 426 15.653 60.418 −0.465 1.00 31.59 A N ATOM 1678 CA THR A 426 15.329 60.773 −1.838 1.00 31.80 A C ATOM 1679 CB THR A 426 15.512 62.293 −2.081 1.00 32.79 A C ATOM 1680 OG1 THR A 426 15.015 62.645 −3.380 1.00 30.88 A O ATOM 1681 CG2 THR A 426 16.975 62.675 −1.987 1.00 30.39 A C ATOM 1682 C THR A 426 16.267 60.019 −2.756 1.00 31.70 A C ATOM 1683 O THR A 426 17.390 59.698 −2.371 1.00 28.98 A O ATOM 1684 N GLU A 427 15.810 59.737 −3.972 1.00 34.15 A N ATOM 1685 CA GLU A 427 16.706 59.236 −5.012 1.00 35.81 A C ATOM 1686 CB GLU A 427 16.096 58.031 −5.731 1.00 40.71 A C ATOM 1687 CG GLU A 427 16.002 56.804 −4.837 1.00 45.17 A C ATOM 1688 CD GLU A 427 15.363 55.619 −5.519 1.00 54.28 A C ATOM 1689 OE1 GLU A 427 14.396 55.818 −6.282 1.00 56.04 A O ATOM 1690 OE2 GLU A 427 15.824 54.485 −5.277 1.00 60.76 A O ATOM 1691 C GLU A 427 17.068 60.349 −5.995 1.00 33.37 A C ATOM 1692 O GLU A 427 17.986 60.203 −6.798 1.00 35.70 A O ATOM 1693 N GLY A 428 16.351 61.466 −5.920 1.00 33.02 A N ATOM 1694 CA GLY A 428 16.675 62.620 −6.736 1.00 29.12 A C ATOM 1695 C GLY A 428 18.001 63.251 −6.334 1.00 29.53 A C ATOM 1696 O GLY A 428 18.547 62.971 −5.260 1.00 29.95 A O ATOM 1697 N PRO A 429 18.527 64.129 −7.188 1.00 28.08 A N ATOM 1698 CD PRO A 429 17.978 64.559 −8.492 1.00 27.74 A C ATOM 1699 CA PRO A 429 19.759 64.839 −6.822 1.00 23.77 A C ATOM 1700 CB PRO A 429 19.944 65.836 −7.973 1.00 23.62 A C ATOM 1701 CG PRO A 429 19.165 65.253 −9.142 1.00 23.77 A C ATOM 1702 C PRO A 429 19.555 65.586 −5.485 1.00 26.51 A C ATOM 1703 O PRO A 429 18.563 66.288 −5.321 1.00 25.62 A O ATOM 1704 N PRO A 430 20.479 65.424 −4.530 1.00 25.53 A N ATOM 1705 CD PRO A 430 21.665 64.544 −4.578 1.00 22.21 A C ATOM 1706 CA PRO A 430 20.254 66.005 −3.189 1.00 23.15 A C ATOM 1707 CB PRO A 430 21.440 65.468 −2.369 1.00 22.53 A C ATOM 1708 CG PRO A 430 21.871 64.181 −3.115 1.00 25.11 A C ATOM 1709 C PRO A 430 20.222 67.542 −3.147 1.00 24.01 A C ATOM 1710 O PRO A 430 19.482 68.095 −2.337 1.00 22.83 A O ATOM 1711 N LEU A 431 20.991 68.234 −3.987 1.00 23.27 A N ATOM 1712 CA LEU A 431 21.052 69.701 −3.885 1.00 25.99 A C ATOM 1713 CB LEU A 431 22.315 70.274 −4.550 1.00 25.49 A C ATOM 1714 CG LEU A 431 23.675 69.929 −3.939 1.00 28.77 A C ATOM 1715 CD1 LEU A 431 24.819 70.554 −4.737 1.00 18.67 A C ATOM 1716 CD2 LEU A 431 23.738 70.396 −2.496 1.00 22.61 A C ATOM 1717 C LEU A 431 19.823 70.384 −4.476 1.00 26.35 A C ATOM 1718 O LEU A 431 19.279 69.940 −5.473 1.00 24.35 A O ATOM 1719 N HIS A 432 19.393 71.469 −3.842 1.00 26.81 A N ATOM 1720 CA HIS A 432 18.326 72.312 −4.372 1.00 24.94 A C ATOM 1721 CB HIS A 432 17.054 72.196 −3.511 1.00 25.02 A C ATOM 1722 CG HIS A 432 16.385 70.862 −3.627 1.00 28.67 A C ATOM 1723 CD2 HIS A 432 15.220 70.495 −4.203 1.00 27.83 A C ATOM 1724 ND1 HIS A 432 16.959 69.701 −3.150 1.00 29.09 A N ATOM 1725 CE1 HIS A 432 16.165 68.682 −3.419 1.00 26.93 A C ATOM 1726 NE2 HIS A 432 15.108 69.133 −4.060 1.00 27.71 A N ATOM 1727 C HIS A 432 18.805 73.753 −4.431 1.00 23.99 A C ATOM 1728 O HIS A 432 19.857 74.081 −3.890 1.00 27.97 A O ATOM 1729 N LYS A 433 18.030 74.607 −5.089 1.00 26.76 A N ATOM 1730 CA LYS A 433 18.389 76.008 −5.257 1.00 26.56 A C ATOM 1731 CB LYS A 433 17.193 76.792 −5.818 1.00 24.67 A C ATOM 1732 CG LYS A 433 16.782 76.354 −7.227 1.00 21.91 A C ATOM 1733 CD LYS A 433 15.378 76.829 −7.612 1.00 27.01 A C ATOM 1734 CE LYS A 433 15.062 76.579 −9.105 1.00 30.42 A C ATOM 1735 NZ LYS A 433 16.004 77.295 −10.041 1.00 23.69 A N ATOM 1736 C LYS A 433 18.859 76.614 −3.940 1.00 27.97 A C ATOM 1737 O LYS A 433 19.905 77.264 −3.878 1.00 27.51 A O ATOM 1738 N ASP A 434 18.102 76.371 −2.876 1.00 27.28 A N ATOM 1739 CA ASP A 434 18.418 76.986 −1.595 1.00 24.01 A C ATOM 1740 CB ASP A 434 17.364 76.648 −0.538 1.00 27.46 A C ATOM 1741 CG ASP A 434 17.408 77.604 0.626 1.00 28.18 A C ATOM 1742 OD1 ASP A 434 17.232 78.811 0.382 1.00 29.69 A O ATOM 1743 OD2 ASP A 434 17.666 77.158 1.768 1.00 30.91 A O ATOM 1744 C ASP A 434 19.808 76.616 −1.091 1.00 26.06 A C ATOM 1745 O ASP A 434 20.517 77.444 −0.525 1.00 25.00 A O ATOM 1746 N ASP A 435 20.191 75.365 −1.284 1.00 25.29 A N ATOM 1747 CA ASP A 435 21.499 74.902 −0.845 1.00 25.22 A C ATOM 1748 CB ASP A 435 21.591 73.368 −0.972 1.00 26.96 A C ATOM 1749 CG ASP A 435 20.433 72.643 −0.268 1.00 24.70 A C ATOM 1750 OD1 ASP A 435 20.201 72.899 0.923 1.00 26.62 A O ATOM 1751 OD2 ASP A 435 19.762 71.804 −0.901 1.00 26.76 A O ATOM 1752 C ASP A 435 22.619 75.575 −1.654 1.00 26.00 A C ATOM 1753 O ASP A 435 23.652 75.968 −1.098 1.00 25.44 A O ATOM 1754 N VAL A 436 22.406 75.688 −2.966 1.00 27.05 A N ATOM 1755 CA VAL A 436 23.402 76.237 −3.898 1.00 26.76 A C ATOM 1756 CB VAL A 436 22.992 75.995 −5.366 1.00 28.44 A C ATOM 1757 CG1 VAL A 436 23.963 76.717 −6.357 1.00 28.54 A C ATOM 1758 CG2 VAL A 436 22.917 74.476 −5.649 1.00 25.57 A C ATOM 1759 C VAL A 436 23.628 77.727 −3.654 1.00 27.87 A C ATOM 1760 O VAL A 436 24.759 78.181 −3.512 1.00 30.24 A O ATOM 1761 N ASN A 437 22.539 78.479 −3.600 1.00 27.85 A N ATOM 1762 CA ASN A 437 22.614 79.884 −3.260 1.00 31.33 A C ATOM 1763 CB ASN A 437 21.240 80.533 −3.366 1.00 32.53 A C ATOM 1764 CG ASN A 437 20.748 80.626 −4.799 1.00 35.79 A C ATOM 1765 OD1 ASN A 437 21.510 80.422 −5.759 1.00 35.87 A O ATOM 1766 ND2 ASN A 437 19.472 80.930 −4.953 1.00 35.07 A N ATOM 1767 C ASN A 437 23.187 80.081 −1.863 1.00 31.99 A C ATOM 1768 O ASN A 437 23.964 81.011 −1.641 1.00 30.29 A O ATOM 1769 N GLY A 438 22.811 79.209 −0.927 1.00 28.34 A N ATOM 1770 CA GLY A 438 23.367 79.276 0.419 1.00 26.93 A C ATOM 1771 C GLY A 438 24.888 79.230 0.372 1.00 32.48 A C ATOM 1772 O GLY A 438 25.576 80.091 0.920 1.00 33.32 A O ATOM 1773 N ILE A 439 25.423 78.228 −0.316 1.00 29.69 A N ATOM 1774 CA ILE A 439 26.866 78.075 −0.435 1.00 32.74 A C ATOM 1775 CB ILE A 439 27.243 76.653 −0.928 1.00 29.49 A C ATOM 1776 CG2 ILE A 439 27.078 76.554 −2.418 1.00 29.33 A C ATOM 1777 CG1 ILE A 439 28.658 76.275 −0.481 1.00 33.29 A C ATOM 1778 CD1 ILE A 439 28.815 76.145 1.043 1.00 28.96 A C ATOM 1779 C ILE A 439 27.510 79.165 −1.323 1.00 34.07 A C ATOM 1780 O ILE A 439 28.644 79.574 −1.067 1.00 35.20 A O ATOM 1781 N ARG A 440 26.794 79.635 −2.347 1.00 32.49 A N ATOM 1782 CA ARG A 440 27.293 80.720 −3.201 1.00 36.62 A C ATOM 1783 CB ARG A 440 26.357 81.000 −4.382 1.00 35.67 A C ATOM 1784 CG ARG A 440 26.545 80.111 −5.586 1.00 37.21 A C ATOM 1785 CD ARG A 440 25.742 80.663 −6.747 1.00 40.92 A C ATOM 1786 NE ARG A 440 26.563 81.391 −7.718 1.00 39.70 A N ATOM 1787 CZ ARG A 440 26.137 81.726 −8.933 1.00 37.75 A C ATOM 1788 NH1 ARG A 440 24.902 81.402 −9.306 1.00 39.48 A N ATOM 1789 NH2 ARG A 440 26.935 82.374 −9.778 1.00 37.83 A N ATOM 1790 C ARG A 440 27.461 82.007 −2.419 1.00 38.89 A C ATOM 1791 O ARG A 440 28.368 82.798 −2.693 1.00 41.04 A O ATOM 1792 N HIS A 441 26.564 82.218 −1.460 1.00 38.38 A N ATOM 1793 CA HIS A 441 26.593 83.407 −0.614 1.00 38.89 A C ATOM 1794 CB HIS A 441 25.220 83.658 0.016 1.00 36.58 A C ATOM 1795 CG HIS A 441 24.131 83.878 −0.990 1.00 41.22 A C ATOM 1796 CD2 HIS A 441 22.784 83.916 −0.851 1.00 40.64 A C ATOM 1797 ND1 HIS A 441 24.387 84.086 −2.329 1.00 40.03 A N ATOM 1798 CE1 HIS A 441 23.243 84.245 −2.974 1.00 35.91 A C ATOM 1799 NE2 HIS A 441 22.256 84.146 −2.102 1.00 40.67 A N ATOM 1800 C HIS A 441 27.657 83.317 0.473 1.00 39.63 A C ATOM 1801 O HIS A 441 27.752 84.193 1.323 1.00 42.58 A O ATOM 1802 N LEU A 442 28.464 82.266 0.433 1.00 36.50 A N ATOM 1803 CA LEU A 442 29.542 82.098 1.396 1.00 38.88 A C ATOM 1804 CB LEU A 442 29.395 80.753 2.112 1.00 40.22 A C ATOM 1805 CG LEU A 442 29.497 80.700 3.640 1.00 42.51 A C ATOM 1806 CD1 LEU A 442 28.844 81.915 4.284 1.00 40.07 A C ATOM 1807 CD2 LEU A 442 28.865 79.418 4.164 1.00 29.38 A C ATOM 1808 C LEU A 442 30.914 82.175 0.725 1.00 40.09 A C ATOM 1809 O LEU A 442 31.822 82.834 1.230 1.00 41.93 A O ATOM 1810 N TYR A 443 31.055 81.492 −0.409 1.00 36.48 A N ATOM 1811 CA TYR A 443 32.347 81.345 −1.082 1.00 36.79 A C ATOM 1812 CB TYR A 443 32.706 79.859 −1.193 1.00 34.33 A C ATOM 1813 CG TYR A 443 32.980 79.232 0.155 1.00 40.17 A C ATOM 1814 CD1 TYR A 443 34.209 79.414 0.786 1.00 38.32 A C ATOM 1815 CE1 TYR A 443 34.465 78.857 2.029 1.00 38.03 A C ATOM 1816 CD2 TYR A 443 32.008 78.479 0.811 1.00 35.43 A C ATOM 1817 CE2 TYR A 443 32.264 77.913 2.053 1.00 34.75 A C ATOM 1818 CZ TYR A 443 33.489 78.111 2.655 1.00 33.20 A C ATOM 1819 OH TYR A 443 33.760 77.551 3.880 1.00 34.31 A O ATOM 1820 C TYR A 443 32.404 82.003 −2.460 1.00 41.08 A C ATOM 1821 O TYR A 443 31.394 82.093 −3.160 1.00 45.49 A O ATOM 1822 ZN ZN A 500 21.993 69.936 10.164 1.00 28.09 A Zn ATOM 1823 ZN ZN A 501 30.069 64.692 18.116 1.00 38.01 A Zn ATOM 1824 CA CA A 502 20.361 58.697 17.246 1.00 39.90 A Ca ATOM 1825 CA CA A 504 38.504 70.165 12.384 1.00 55.43 A Ca ATOM 1826 CA CA A 505 41.479 78.513 7.460 1.00 53.78 A Ca TER 1827 CA A 505 ATOM 1828 CB ASP B 41 4.599 14.284 39.348 1.00 57.62 B C ATOM 1829 CG ASP B 41 3.860 14.557 38.068 1.00 57.64 B C ATOM 1830 OD1 ASP B 41 3.948 13.726 37.138 1.00 55.33 B O ATOM 1831 OD2 ASP B 41 3.204 15.614 37.987 1.00 62.09 B O ATOM 1832 C ASP B 41 5.553 16.517 40.010 1.00 59.56 B C ATOM 1833 O ASP B 41 5.888 17.526 39.379 1.00 59.73 B O ATOM 1834 N ASP B 41 6.829 14.438 40.326 1.00 54.69 B N ATOM 1835 CA ASP B 41 5.869 15.118 39.474 1.00 56.03 B C ATOM 1836 N ARG B 42 4.909 16.572 41.172 1.00 59.41 B N ATOM 1837 CA ARG B 42 4.698 17.830 41.880 1.00 58.55 B C ATOM 1838 CB ARG B 42 3.982 17.574 43.208 1.00 62.12 B C ATOM 1839 CG ARG B 42 4.020 18.752 44.178 1.00 62.32 B C ATOM 1840 CD ARG B 42 2.617 19.297 44.434 1.00 67.97 B C ATOM 1841 NE ARG B 42 2.635 20.627 45.043 1.00 69.68 B N ATOM 1842 CZ ARG B 42 1.646 21.512 44.937 1.00 67.45 B C ATOM 1843 NH1 ARG B 42 0.558 21.212 44.236 1.00 61.67 B N ATOM 1844 NH2 ARG B 42 1.747 22.698 45.524 1.00 66.36 B N ATOM 1845 C ARG B 42 6.056 18.454 42.155 1.00 59.93 B C ATOM 1846 O ARG B 42 6.218 19.677 42.151 1.00 58.05 B O ATOM 1847 N GLN B 43 7.026 17.579 42.401 1.00 57.91 B N ATOM 1848 CA GLN B 43 8.398 17.965 42.665 1.00 55.81 B C ATOM 1849 CB GLN B 43 9.231 16.716 42.983 1.00 59.15 B C ATOM 1850 CG GLN B 43 8.508 15.657 43.840 1.00 61.71 B C ATOM 1851 CD GLN B 43 7.720 14.633 43.015 1.00 60.78 B C ATOM 1852 OE1 GLN B 43 8.284 13.914 42.185 1.00 61.04 B O ATOM 1853 NE2 GLN B 43 6.414 14.552 43.261 1.00 58.24 B N ATOM 1854 C GLN B 43 8.961 18.654 41.428 1.00 58.12 B C ATOM 1855 O GLN B 43 9.605 19.704 41.508 1.00 54.51 B O ATOM 1856 N LEU B 44 8.712 18.041 40.279 1.00 54.46 B N ATOM 1857 CA LEU B 44 9.204 18.570 39.028 1.00 52.46 B C ATOM 1858 CB LEU B 44 8.745 17.681 37.874 1.00 52.72 B C ATOM 1859 CG LEU B 44 9.715 17.529 36.704 1.00 56.91 B C ATOM 1860 CD1 LEU B 44 9.225 16.459 35.728 1.00 52.04 B C ATOM 1861 CD2 LEU B 44 9.940 18.866 36.003 1.00 53.29 B C ATOM 1862 C LEU B 44 8.686 19.991 38.839 1.00 50.96 B C ATOM 1863 O LEU B 44 9.464 20.929 38.676 1.00 49.90 B O ATOM 1864 N ALA B 45 7.368 20.147 38.870 1.00 50.63 B N ATOM 1865 CA ALA B 45 6.753 21.432 38.582 1.00 47.02 B C ATOM 1866 CB ALA B 45 5.249 21.324 38.701 1.00 51.53 B C ATOM 1867 C ALA B 45 7.272 22.535 39.490 1.00 49.21 B C ATOM 1868 O ALA B 45 7.424 23.682 39.067 1.00 46.48 B O ATOM 1869 N GLU B 46 7.535 22.195 40.744 1.00 48.02 B N ATOM 1870 CA GLU B 46 7.964 23.197 41.698 1.00 46.08 B C ATOM 1871 CB GLU B 46 7.862 22.655 43.124 1.00 52.26 B C ATOM 1872 CG GLU B 46 6.438 22.299 43.523 1.00 55.18 B C ATOM 1873 CD GLU B 46 6.297 21.930 44.991 1.00 62.40 B C ATOM 1874 OE1 GLU B 46 7.317 21.617 45.650 1.00 58.01 B O ATOM 1875 OE2 GLU B 46 5.150 21.952 45.485 1.00 63.52 B O ATOM 1876 C GLU B 46 9.376 23.661 41.396 1.00 42.57 B C ATOM 1877 O GLU B 46 9.659 24.858 41.401 1.00 42.61 B O ATOM 1878 N GLU B 47 10.259 22.706 41.131 1.00 44.28 B N ATOM 1879 CA GLU B 47 11.657 22.990 40.809 1.00 49.40 B C ATOM 1880 CB GLU B 47 12.387 21.659 40.637 1.00 51.72 B C ATOM 1881 CG GLU B 47 13.897 21.735 40.681 1.00 56.10 B C ATOM 1882 CD GLU B 47 14.524 20.387 41.011 1.00 66.64 B C ATOM 1883 OE1 GLU B 47 13.865 19.573 41.701 1.00 65.29 B O ATOM 1884 OE2 GLU B 47 15.677 20.145 40.587 1.00 66.73 B O ATOM 1885 C GLU B 47 11.811 23.851 39.534 1.00 43.51 B C ATOM 1886 O GLU B 47 12.550 24.836 39.511 1.00 37.90 B O ATOM 1887 N TYR B 48 11.091 23.469 38.488 1.00 41.74 B N ATOM 1888 CA TYR B 48 11.130 24.149 37.195 1.00 40.24 B C ATOM 1889 CB TYR B 48 10.198 23.410 36.237 1.00 40.91 B C ATOM 1890 CG TYR B 48 10.361 23.711 34.765 1.00 40.48 B C ATOM 1891 CD1 TYR B 48 9.809 24.858 34.202 1.00 39.11 B C ATOM 1892 CE1 TYR B 48 9.942 25.123 32.847 1.00 37.45 B C ATOM 1893 CD2 TYR B 48 11.028 22.822 33.929 1.00 36.30 B C ATOM 1894 CE2 TYR B 48 11.163 23.069 32.583 1.00 36.08 B C ATOM 1895 CZ TYR B 48 10.619 24.219 32.046 1.00 38.86 B C ATOM 1896 OH TYR B 48 10.745 24.464 30.708 1.00 33.22 B O ATOM 1897 C TYR B 48 10.692 25.607 37.335 1.00 41.99 B C ATOM 1898 O TYR B 48 11.426 26.533 36.979 1.00 40.32 B O ATOM 1899 N LEU B 49 9.495 25.805 37.868 1.00 38.21 B N ATOM 1900 CA LEU B 49 8.939 27.132 38.035 1.00 36.75 B C ATOM 1901 CB LEU B 49 7.582 27.030 38.720 1.00 41.86 B C ATOM 1902 CG LEU B 49 6.513 26.287 37.921 1.00 43.82 B C ATOM 1903 CD1 LEU B 49 5.430 25.739 38.829 1.00 47.45 B C ATOM 1904 CD2 LEU B 49 5.917 27.201 36.856 1.00 44.02 B C ATOM 1905 C LEU B 49 9.856 28.070 38.813 1.00 42.56 B C ATOM 1906 O LEU B 49 9.903 29.274 38.543 1.00 42.28 B O ATOM 1907 N TYR B 50 10.580 27.541 39.792 1.00 39.79 B N ATOM 1908 CA TYR B 50 11.465 28.403 40.562 1.00 40.23 B C ATOM 1909 CB TYR B 50 11.781 27.805 41.937 1.00 44.39 B C ATOM 1910 CG TYR B 50 13.052 28.356 42.560 1.00 43.40 B C ATOM 1911 CD1 TYR B 50 13.034 29.524 43.318 1.00 47.11 B C ATOM 1912 CE1 TYR B 50 14.203 30.033 43.890 1.00 46.40 B C ATOM 1913 CD2 TYR B 50 14.272 27.710 42.385 1.00 43.80 B C ATOM 1914 CE2 TYR B 50 15.450 28.207 42.956 1.00 47.67 B C ATOM 1915 CZ TYR B 50 15.409 29.367 43.705 1.00 48.90 B C ATOM 1916 OH TYR B 50 16.574 29.852 44.268 1.00 49.50 B O ATOM 1917 C TYR B 50 12.751 28.635 39.809 1.00 39.91 B C ATOM 1918 O TYR B 50 13.223 29.761 39.680 1.00 41.02 B O ATOM 1919 N ARG B 51 13.331 27.545 39.335 1.00 40.60 B N ATOM 1920 CA ARG B 51 14.602 27.596 38.635 1.00 40.66 B C ATOM 1921 CB ARG B 51 14.938 26.209 38.109 1.00 37.44 B C ATOM 1922 CG ARG B 51 16.150 26.145 37.267 1.00 38.53 B C ATOM 1923 CD ARG B 51 16.238 24.792 36.596 1.00 41.46 B C ATOM 1924 NE ARG B 51 16.714 23.760 37.504 1.00 43.17 B N ATOM 1925 CZ ARG B 51 17.994 23.589 37.801 1.00 41.52 B C ATOM 1926 NH1 ARG B 51 18.898 24.399 37.273 1.00 44.30 B N ATOM 1927 NH2 ARG B 51 18.367 22.628 38.637 1.00 44.40 B N ATOM 1928 C ARG B 51 14.557 28.585 37.482 1.00 37.89 B C ATOM 1929 O ARG B 51 15.497 29.336 37.265 1.00 38.49 B O ATOM 1930 N TYR B 52 13.450 28.603 36.752 1.00 37.43 B N ATOM 1931 CA TYR B 52 13.388 29.418 35.543 1.00 37.67 B C ATOM 1932 CB TYR B 52 12.773 28.618 34.386 1.00 32.61 B C ATOM 1933 CG TYR B 52 13.618 27.405 34.072 1.00 33.86 B C ATOM 1934 CD1 TYR B 52 13.144 26.118 34.285 1.00 32.11 B C ATOM 1935 CE1 TYR B 52 13.940 25.013 34.013 1.00 33.86 B C ATOM 1936 CD2 TYR B 52 14.928 27.557 33.615 1.00 32.24 B C ATOM 1937 CE2 TYR B 52 15.723 26.478 33.348 1.00 29.22 B C ATOM 1938 CZ TYR B 52 15.232 25.209 33.545 1.00 31.85 B C ATOM 1939 OH TYR B 52 16.055 24.144 33.279 1.00 32.52 B O ATOM 1940 C TYR B 52 12.732 30.777 35.744 1.00 39.64 B C ATOM 1941 O TYR B 52 12.510 31.502 34.782 1.00 38.67 B O ATOM 1942 N GLY B 53 12.430 31.116 37.002 1.00 41.82 B N ATOM 1943 CA GLY B 53 11.996 32.458 37.371 1.00 42.70 B C ATOM 1944 C GLY B 53 10.498 32.733 37.456 1.00 44.52 B C ATOM 1945 O GLY B 53 10.075 33.861 37.720 1.00 40.63 B O ATOM 1946 N TYR B 54 9.692 31.705 37.229 1.00 41.43 B N ATOM 1947 CA TYR B 54 8.250 31.870 37.161 1.00 43.82 B C ATOM 1948 CB TYR B 54 7.619 30.628 36.536 1.00 43.57 B C ATOM 1949 CG TYR B 54 8.004 30.430 35.077 1.00 43.55 B C ATOM 1950 CD1 TYR B 54 8.997 29.522 34.704 1.00 43.54 B C ATOM 1951 CE1 TYR B 54 9.345 29.347 33.368 1.00 38.02 B C ATOM 1952 CD2 TYR B 54 7.377 31.160 34.076 1.00 43.19 B C ATOM 1953 CE2 TYR B 54 7.720 30.997 32.751 1.00 44.48 B C ATOM 1954 CZ TYR B 54 8.699 30.088 32.400 1.00 40.27 B C ATOM 1955 OH TYR B 54 9.021 29.936 31.074 1.00 39.85 B O ATOM 1956 C TYR B 54 7.612 32.196 38.526 1.00 50.04 B C ATOM 1957 O TYR B 54 6.844 33.156 38.657 1.00 44.74 B O ATOM 1958 N THR B 55 7.935 31.400 39.538 1.00 47.55 B N ATOM 1959 CA THR B 55 7.424 31.648 40.881 1.00 44.74 B C ATOM 1960 CB THR B 55 7.946 30.601 41.882 1.00 43.88 B C ATOM 1961 OG1 THR B 55 9.334 30.833 42.132 1.00 53.17 B O ATOM 1962 CG2 THR B 55 7.786 29.196 41.330 1.00 39.70 B C ATOM 1963 C THR B 55 7.790 33.069 41.341 1.00 50.30 B C ATOM 1964 O THR B 55 6.929 33.818 41.801 1.00 51.31 B O ATOM 1965 N ARG B 56 9.054 33.449 41.184 1.00 49.30 B N ATOM 1966 CA ARG B 56 9.517 34.774 41.610 1.00 51.66 B C ATOM 1967 CB ARG B 56 11.016 34.937 41.349 1.00 56.44 B C ATOM 1968 CG ARG B 56 11.667 36.083 42.125 1.00 63.05 B C ATOM 1969 CD ARG B 56 13.044 35.664 42.643 1.00 67.17 B C ATOM 1970 NE ARG B 56 13.734 36.716 43.388 1.00 66.86 B N ATOM 1971 CZ ARG B 56 15.058 36.833 43.456 1.00 70.07 B C ATOM 1972 NH1 ARG B 56 15.835 35.970 42.808 1.00 68.46 B N ATOM 1973 NH2 ARG B 56 15.609 37.818 44.159 1.00 70.07 B N ATOM 1974 C ARG B 56 8.747 35.928 40.962 1.00 57.09 B C ATOM 1975 O ARG B 56 8.488 36.944 41.602 1.00 54.17 B O ATOM 1976 N VAL B 57 8.398 35.780 39.689 1.00 54.28 B N ATOM 1977 CA VAL B 57 7.579 36.784 39.023 1.00 54.64 B C ATOM 1978 CB VAL B 57 7.458 36.516 37.529 1.00 52.07 B C ATOM 1979 CG1 VAL B 57 6.487 37.490 36.911 1.00 52.20 B C ATOM 1980 CG2 VAL B 57 8.801 36.629 36.872 1.00 50.30 B C ATOM 1981 C VAL B 57 6.173 36.771 39.599 1.00 58.23 B C ATOM 1982 O VAL B 57 5.616 37.817 39.946 1.00 59.62 B O ATOM 1983 N ALA B 58 5.605 35.571 39.677 1.00 54.58 B N ATOM 1984 CA ALA B 58 4.266 35.371 40.216 1.00 54.29 B C ATOM 1985 CB ALA B 58 3.945 33.891 40.273 1.00 48.36 B C ATOM 1986 C ALA B 58 4.143 35.998 41.599 1.00 56.31 B C ATOM 1987 O ALA B 58 3.115 36.582 41.933 1.00 61.38 B O ATOM 1988 O GLU B 59 4.760 38.678 44.521 1.00 56.15 B O ATOM 1989 N GLU B 59 5.201 35.873 42.394 1.00 53.35 B N ATOM 1990 CA GLU B 59 5.266 36.483 43.719 1.00 54.16 B C ATOM 1991 C GLU B 59 5.296 38.002 43.646 1.00 56.99 B C ATOM 1992 CB GLU B 59 6.499 35.986 44.480 1.00 47.99 B C ATOM 1993 CG GLU B 59 6.509 34.479 44.677 1.00 50.29 B C ATOM 1994 CD GLU B 59 7.631 33.986 45.573 1.00 46.44 B C ATOM 1995 OE1 GLU B 59 8.714 34.627 45.624 1.00 44.75 B O ATOM 1996 OE2 GLU B 59 7.409 32.944 46.229 1.00 47.26 B O ATOM 1997 O MET B 60 4.516 41.810 42.438 1.00 62.55 B O ATOM 1998 N MET B 60 5.941 38.532 42.609 1.00 58.91 B N ATOM 1999 CA MET B 60 6.063 39.975 42.429 1.00 58.55 B C ATOM 2000 C MET B 60 4.710 40.624 42.167 1.00 62.24 B C ATOM 2001 CB MET B 60 7.020 40.299 41.277 1.00 61.94 B C ATOM 2002 CG MET B 60 8.484 39.994 41.569 1.00 63.88 B C ATOM 2003 SD MET B 60 9.574 40.298 40.156 1.00 75.33 B S ATOM 2004 CE MET B 60 10.580 41.639 40.788 1.00 68.61 B C ATOM 2005 O ARG B 61 0.316 39.387 41.767 1.00 68.92 B O ATOM 2006 N ARG B 61 3.774 39.841 41.641 1.00 64.10 B N ATOM 2007 CA ARG B 61 2.460 40.358 41.274 1.00 66.40 B C ATOM 2008 C ARG B 61 1.377 39.830 42.212 1.00 66.89 B C ATOM 2009 CB ARG B 61 2.137 39.967 39.832 1.00 65.83 B C ATOM 2010 CG ARG B 61 3.197 40.391 38.818 1.00 64.20 B C ATOM 2011 CD ARG B 61 3.435 39.299 37.784 1.00 63.60 B C ATOM 2012 NE ARG B 61 4.201 39.774 36.635 1.00 67.07 B N ATOM 2013 CZ ARG B 61 3.667 40.089 35.458 1.00 71.36 B C ATOM 2014 NH1 ARG B 61 2.356 39.978 35.271 1.00 69.85 B N ATOM 2015 NH2 ARG B 61 4.441 40.511 34.463 1.00 71.44 B N ATOM 2016 O GLY B 62 1.784 37.218 43.983 1.00 67.43 B O ATOM 2017 N GLY B 62 1.643 39.884 43.513 1.00 65.11 B N ATOM 2018 CA GLY B 62 0.736 39.304 44.484 1.00 65.49 B C ATOM 2019 C GLY B 62 0.772 37.789 44.386 1.00 68.91 B C ATOM 2020 O GLU B 63 0.939 33.877 45.731 1.00 69.33 B O ATOM 2021 N GLU B 63 −0.333 37.137 44.737 1.00 71.67 B N ATOM 2022 CA GLU B 63 −0.380 35.675 44.791 1.00 70.54 B C ATOM 2023 C GLU B 63 0.748 35.098 45.654 1.00 68.20 B C ATOM 2024 CB GLU B 63 −0.343 35.061 43.387 1.00 63.60 B C ATOM 2025 CG GLU B 63 −0.594 33.553 43.391 1.00 65.59 B C ATOM 2026 CD GLU B 63 −1.981 33.172 43.937 1.00 63.90 B C ATOM 2027 OE1 GLU B 63 −2.960 33.896 43.649 1.00 57.75 B O ATOM 2028 OE2 GLU B 63 −2.095 32.139 44.638 1.00 60.45 B O ATOM 2029 O ALA B 66 −1.271 26.997 42.798 1.00 69.51 B O ATOM 2030 N ALA B 66 −2.081 28.983 44.548 1.00 54.43 B N ATOM 2031 CA ALA B 66 −0.668 28.661 44.417 1.00 61.59 B C ATOM 2032 C ALA B 66 −0.425 27.807 43.179 1.00 63.17 B C ATOM 2033 CB ALA B 66 −0.161 27.950 45.665 1.00 62.88 B C ATOM 2034 O LEU B 67 0.913 28.041 39.043 1.00 53.98 B O ATOM 2035 N LEU B 67 0.737 27.995 42.563 1.00 59.81 B N ATOM 2036 CA LEU B 67 1.110 27.299 41.327 1.00 61.14 B C ATOM 2037 C LEU B 67 0.327 27.783 40.097 1.00 58.49 B C ATOM 2038 CB LEU B 67 0.992 25.777 41.483 1.00 57.74 B C ATOM 2039 CG LEU B 67 2.318 25.013 41.456 1.00 56.56 B C ATOM 2040 CD1 LEU B 67 3.208 25.435 42.608 1.00 54.76 B C ATOM 2041 CD2 LEU B 67 2.090 23.511 41.478 1.00 55.06 B C ATOM 2042 N GLY B 68 −0.992 27.905 40.244 1.00 55.51 B N ATOM 2043 CA GLY B 68 −1.868 28.317 39.157 1.00 53.27 B C ATOM 2044 C GLY B 68 −1.391 29.539 38.394 1.00 58.72 B C ATOM 2045 O GLY B 68 −1.251 29.497 37.163 1.00 57.37 B O ATOM 2046 N PRO B 69 −1.147 30.645 39.116 1.00 58.22 B N ATOM 2047 CD PRO B 69 −1.449 30.823 40.548 1.00 59.15 B C ATOM 2048 CA PRO B 69 −0.615 31.871 38.512 1.00 51.74 B C ATOM 2049 CB PRO B 69 −0.397 32.784 39.720 1.00 58.75 B C ATOM 2050 CG PRO B 69 −1.387 32.309 40.721 1.00 58.35 B C ATOM 2051 C PRO B 69 0.712 31.605 37.806 1.00 53.95 B C ATOM 2052 O PRO B 69 0.822 31.835 36.605 1.00 53.13 B O ATOM 2053 N ALA B 70 1.700 31.118 38.547 1.00 52.50 B N ATOM 2054 CA ALA B 70 3.008 30.835 37.982 1.00 49.69 B C ATOM 2055 CB ALA B 70 3.928 30.202 39.030 1.00 42.95 B C ATOM 2056 C ALA B 70 2.881 29.938 36.754 1.00 50.92 B C ATOM 2057 O ALA B 70 3.554 30.160 35.746 1.00 50.97 B O ATOM 2058 N LEU B 71 2.003 28.943 36.836 1.00 49.67 B N ATOM 2059 CA LEU B 71 1.803 28.001 35.741 1.00 49.52 B C ATOM 2060 CB LEU B 71 0.764 26.948 36.116 1.00 51.84 B C ATOM 2061 CG LEU B 71 1.259 25.674 36.790 1.00 53.46 B C ATOM 2062 CD1 LEU B 71 0.344 24.526 36.415 1.00 54.90 B C ATOM 2063 CD2 LEU B 71 2.666 25.357 36.370 1.00 49.49 B C ATOM 2064 C LEU B 71 1.356 28.688 34.454 1.00 50.77 B C ATOM 2065 O LEU B 71 1.780 28.317 33.355 1.00 44.45 B O ATOM 2066 N LEU B 72 0.469 29.669 34.595 1.00 51.46 B N ATOM 2067 CA LEU B 72 −0.071 30.370 33.437 1.00 53.21 B C ATOM 2068 CB LEU B 72 −1.257 31.250 33.835 1.00 49.12 B C ATOM 2069 CG LEU B 72 −2.442 31.203 32.867 1.00 53.99 B C ATOM 2070 CD1 LEU B 72 −2.909 29.774 32.661 1.00 54.77 B C ATOM 2071 CD2 LEU B 72 −3.588 32.073 33.352 1.00 61.28 B C ATOM 2072 C LEU B 72 1.017 31.219 32.795 1.00 48.74 B C ATOM 2073 O LEU B 72 1.030 31.415 31.586 1.00 47.12 B O ATOM 2074 N LEU B 73 1.913 31.733 33.629 1.00 45.48 B N ATOM 2075 CA LEU B 73 3.025 32.541 33.166 1.00 49.85 B C ATOM 2076 CB LEU B 73 3.795 33.108 34.358 1.00 45.75 B C ATOM 2077 CG LEU B 73 3.137 34.282 35.081 1.00 49.62 B C ATOM 2078 CD1 LEU B 73 4.088 34.861 36.110 1.00 52.10 B C ATOM 2079 CD2 LEU B 73 2.722 35.344 34.074 1.00 52.25 B C ATOM 2080 C LEU B 73 3.949 31.690 32.308 1.00 44.51 B C ATOM 2081 O LEU B 73 4.547 32.164 31.350 1.00 40.49 B O ATOM 2082 N LEU B 74 4.043 30.423 32.678 1.00 44.12 B N ATOM 2083 CA LEU B 74 4.913 29.470 32.015 1.00 45.83 B C ATOM 2084 CB LEU B 74 5.113 28.263 32.926 1.00 40.02 B C ATOM 2085 CG LEU B 74 5.880 27.067 32.408 1.00 40.81 B C ATOM 2086 CD1 LEU B 74 6.625 26.415 33.563 1.00 41.20 B C ATOM 2087 CD2 LEU B 74 4.934 26.087 31.752 1.00 42.10 B C ATOM 2088 C LEU B 74 4.323 29.037 30.685 1.00 44.15 B C ATOM 2089 O LEU B 74 5.023 28.947 29.678 1.00 40.39 B O ATOM 2090 N GLN B 75 3.026 28.760 30.696 1.00 43.25 B N ATOM 2091 CA GLN B 75 2.317 28.344 29.496 1.00 42.66 B C ATOM 2092 CB GLN B 75 0.886 27.922 29.836 1.00 46.75 B C ATOM 2093 CG GLN B 75 0.777 26.503 30.373 1.00 48.30 B C ATOM 2094 CD GLN B 75 −0.382 26.327 31.337 1.00 54.90 B C ATOM 2095 OE1 GLN B 75 −1.137 27.264 31.605 1.00 51.44 B O ATOM 2096 NE2 GLN B 75 −0.522 25.120 31.870 1.00 55.25 B N ATOM 2097 C GLN B 75 2.309 29.456 28.458 1.00 41.94 B C ATOM 2098 O GLN B 75 2.416 29.189 27.266 1.00 42.70 B O ATOM 2099 N LYS B 76 2.174 30.697 28.909 1.00 41.54 B N ATOM 2100 CA LYS B 76 2.229 31.837 27.996 1.00 43.18 B C ATOM 2101 CB LYS B 76 1.822 33.138 28.696 1.00 42.56 B C ATOM 2102 CG LYS B 76 0.399 33.151 29.238 1.00 53.22 B C ATOM 2103 CD LYS B 76 0.061 34.488 29.890 1.00 57.10 B C ATOM 2104 CE LYS B 76 −1.406 34.558 30.309 1.00 55.64 B C ATOM 2105 NZ LYS B 76 −1.683 35.807 31.069 1.00 61.58 B N ATOM 2106 C LYS B 76 3.652 31.979 27.477 1.00 41.32 B C ATOM 2107 O LYS B 76 3.878 32.250 26.298 1.00 41.61 B O ATOM 2108 N GLN B 77 4.608 31.788 28.377 1.00 39.90 B N ATOM 2109 CA GLN B 77 6.016 31.950 28.051 1.00 43.73 B C ATOM 2110 CB GLN B 77 6.853 31.963 29.338 1.00 41.93 B C ATOM 2111 CG GLN B 77 8.316 32.325 29.142 1.00 42.12 B C ATOM 2112 CD GLN B 77 8.520 33.702 28.508 1.00 48.35 B C ATOM 2113 OE1 GLN B 77 7.685 34.605 28.647 1.00 53.58 B O ATOM 2114 NE2 GLN B 77 9.640 33.860 27.804 1.00 44.79 B N ATOM 2115 C GLN B 77 6.508 30.872 27.071 1.00 41.80 B C ATOM 2116 O GLN B 77 7.310 31.157 26.196 1.00 36.58 B O ATOM 2117 N LEU B 78 6.007 29.646 27.203 1.00 40.14 B N ATOM 2118 CA LEU B 78 6.451 28.538 26.358 1.00 37.10 B C ATOM 2119 CB LEU B 78 6.571 27.261 27.185 1.00 36.20 B C ATOM 2120 CG LEU B 78 7.575 27.327 28.334 1.00 36.69 B C ATOM 2121 CD1 LEU B 78 7.725 25.968 28.977 1.00 38.24 B C ATOM 2122 CD2 LEU B 78 8.931 27.811 27.825 1.00 35.45 B C ATOM 2123 C LEU B 78 5.521 28.302 25.163 1.00 39.24 B C ATOM 2124 O LEU B 78 5.641 27.307 24.444 1.00 34.26 B O ATOM 2125 N SER B 79 4.604 29.238 24.953 1.00 42.34 B N ATOM 2126 CA SER B 79 3.545 29.062 23.972 1.00 43.21 B C ATOM 2127 CB SER B 79 4.099 29.225 22.561 1.00 39.70 B C ATOM 2128 OG SER B 79 4.344 30.600 22.323 1.00 39.11 B O ATOM 2129 C SER B 79 2.807 27.732 24.144 1.00 41.66 B C ATOM 2130 O SER B 79 2.634 26.968 23.191 1.00 39.61 B O ATOM 2131 N LEU B 80 2.382 27.468 25.377 1.00 44.88 B N ATOM 2132 CA LEU B 80 1.550 26.307 25.694 1.00 47.95 B C ATOM 2133 CB LEU B 80 2.054 25.611 26.957 1.00 45.82 B C ATOM 2134 CG LEU B 80 3.454 25.020 26.931 1.00 42.34 B C ATOM 2135 CD1 LEU B 80 3.738 24.371 28.272 1.00 46.00 B C ATOM 2136 CD2 LEU B 80 3.592 24.014 25.784 1.00 39.25 B C ATOM 2137 C LEU B 80 0.113 26.755 25.917 1.00 45.17 B C ATOM 2138 O LEU B 80 −0.125 27.922 26.221 1.00 46.92 B O ATOM 2139 N PRO B 81 −0.846 25.829 25.760 1.00 46.80 B N ATOM 2140 CD PRO B 81 −0.628 24.483 25.198 1.00 50.68 B C ATOM 2141 CA PRO B 81 −2.256 26.057 26.103 1.00 51.00 B C ATOM 2142 CB PRO B 81 −2.848 24.648 26.056 1.00 53.70 B C ATOM 2143 CG PRO B 81 −2.026 23.943 25.033 1.00 53.27 B C ATOM 2144 C PRO B 81 −2.366 26.610 27.518 1.00 50.89 B C ATOM 2145 O PRO B 81 −1.925 25.939 28.457 1.00 53.09 B O ATOM 2146 N GLU B 82 −2.949 27.799 27.664 1.00 49.69 B N ATOM 2147 CA GLU B 82 −2.903 28.538 28.923 1.00 51.37 B C ATOM 2148 CB GLU B 82 −2.983 30.031 28.625 1.00 52.24 B C ATOM 2149 CG GLU B 82 −2.193 30.402 27.385 1.00 50.97 B C ATOM 2150 CD GLU B 82 −1.935 31.888 27.253 1.00 55.70 B C ATOM 2151 OE1 GLU B 82 −2.318 32.637 28.173 1.00 55.48 B O ATOM 2152 OE2 GLU B 82 −1.336 32.306 26.231 1.00 57.32 B O ATOM 2153 C GLU B 82 −3.976 28.102 29.930 1.00 57.05 B C ATOM 2154 O GLU B 82 −4.798 28.904 30.380 1.00 56.14 B O ATOM 2155 N THR B 83 −3.942 26.823 30.289 1.00 55.88 B N ATOM 2156 CA THR B 83 −4.939 26.237 31.170 1.00 55.16 B C ATOM 2157 CB THR B 83 −4.854 24.705 31.141 1.00 52.64 B C ATOM 2158 OG1 THR B 83 −3.620 24.282 31.730 1.00 53.23 B O ATOM 2159 CG2 THR B 83 −4.936 24.198 29.725 1.00 48.41 B C ATOM 2160 C THR B 83 −4.792 26.708 32.618 1.00 59.57 B C ATOM 2161 O THR B 83 −5.785 26.977 33.307 1.00 56.85 B O ATOM 2162 N GLY B 84 −3.551 26.798 33.082 1.00 57.88 B N ATOM 2163 CA GLY B 84 −3.293 27.156 34.462 1.00 53.25 B C ATOM 2164 C GLY B 84 −3.178 25.904 35.300 1.00 58.09 B C ATOM 2165 O GLY B 84 −3.139 25.963 36.530 1.00 56.84 B O ATOM 2166 N GLU B 85 −3.118 24.759 34.628 1.00 57.50 B N ATOM 2167 CA GLU B 85 −3.043 23.483 35.323 1.00 56.58 B C ATOM 2168 CB GLU B 85 −4.232 22.610 34.952 1.00 57.69 B C ATOM 2169 CG GLU B 85 −5.548 23.118 35.486 1.00 60.69 B C ATOM 2170 CD GLU B 85 −6.626 22.069 35.380 1.00 68.60 B C ATOM 2171 OE1 GLU B 85 −6.329 20.988 34.822 1.00 64.33 B O ATOM 2172 OE2 GLU B 85 −7.758 22.320 35.850 1.00 66.09 B O ATOM 2173 C GLU B 85 −1.754 22.729 35.033 1.00 57.49 B C ATOM 2174 O GLU B 85 −1.144 22.896 33.976 1.00 57.69 B O ATOM 2175 N LEU B 86 −1.348 21.900 35.987 1.00 51.25 B N ATOM 2176 CA LEU B 86 −0.186 21.048 35.825 1.00 57.10 B C ATOM 2177 CB LEU B 86 0.321 20.579 37.191 1.00 52.95 B C ATOM 2178 CG LEU B 86 1.685 19.890 37.227 1.00 56.27 B C ATOM 2179 CD1 LEU B 86 2.152 19.687 38.661 1.00 55.47 B C ATOM 2180 CD2 LEU B 86 2.692 20.714 36.449 1.00 55.68 B C ATOM 2181 C LEU B 86 −0.564 19.866 34.937 1.00 59.82 B C ATOM 2182 O LEU B 86 −0.310 18.707 35.272 1.00 58.79 B O ATOM 2183 N ASP B 87 −1.166 20.181 33.794 1.00 57.78 B N ATOM 2184 CA ASP B 87 −1.700 19.176 32.888 1.00 54.79 B C ATOM 2185 CB ASP B 87 −2.772 19.801 31.991 1.00 58.32 B C ATOM 2186 CG ASP B 87 −2.245 20.966 31.178 1.00 58.74 B C ATOM 2187 OD1 ASP B 87 −2.875 22.048 31.210 1.00 58.51 B O ATOM 2188 OD2 ASP B 87 −1.199 20.803 30.512 1.00 61.56 B O ATOM 2189 C ASP B 87 −0.643 18.489 32.028 1.00 58.98 B C ATOM 2190 O ASP B 87 0.559 18.720 32.171 1.00 60.39 B O ATOM 2191 N SER B 88 −1.119 17.657 31.112 1.00 58.32 B N ATOM 2192 CA SER B 88 −0.268 16.819 30.285 1.00 55.29 B C ATOM 2193 CB SER B 88 −1.146 15.907 29.427 1.00 56.71 B C ATOM 2194 OG SER B 88 −0.367 15.042 28.619 1.00 60.79 B O ATOM 2195 C SER B 88 0.694 17.614 29.395 1.00 55.84 B C ATOM 2196 O SER B 88 1.862 17.254 29.261 1.00 53.72 B O ATOM 2197 N ALA B 89 0.202 18.680 28.776 1.00 57.35 B N ATOM 2198 CA ALA B 89 1.035 19.471 27.874 1.00 56.74 B C ATOM 2199 CB ALA B 89 0.233 20.606 27.261 1.00 50.94 B C ATOM 2200 C ALA B 89 2.203 20.030 28.654 1.00 53.67 B C ATOM 2201 O ALA B 89 3.359 19.941 28.235 1.00 54.21 B O ATOM 2202 N THR B 90 1.875 20.607 29.802 1.00 51.49 B N ATOM 2203 CA THR B 90 2.837 21.285 30.648 1.00 51.97 B C ATOM 2204 CB THR B 90 2.132 21.947 31.835 1.00 53.28 B C ATOM 2205 OG1 THR B 90 0.985 22.678 31.367 1.00 51.93 B O ATOM 2206 CG2 THR B 90 3.082 22.884 32.549 1.00 51.40 B C ATOM 2207 C THR B 90 3.910 20.332 31.162 1.00 50.55 B C ATOM 2208 O THR B 90 5.096 20.640 31.124 1.00 45.84 B O ATOM 2209 N LEU B 91 3.480 19.172 31.641 1.00 51.37 B N ATOM 2210 CA LEU B 91 4.390 18.161 32.164 1.00 48.46 B C ATOM 2211 CB LEU B 91 3.586 16.970 32.679 1.00 57.50 B C ATOM 2212 CG LEU B 91 3.634 16.648 34.172 1.00 51.59 B C ATOM 2213 CD1 LEU B 91 3.506 17.911 34.993 1.00 54.20 B C ATOM 2214 CD2 LEU B 91 2.533 15.660 34.521 1.00 55.95 B C ATOM 2215 C LEU B 91 5.406 17.681 31.122 1.00 48.37 B C ATOM 2216 O LEU B 91 6.588 17.491 31.425 1.00 46.48 B O ATOM 2217 N LYS B 92 4.942 17.461 29.899 1.00 46.74 B N ATOM 2218 CA LYS B 92 5.848 17.070 28.836 1.00 49.90 B C ATOM 2219 CB LYS B 92 5.086 16.765 27.553 1.00 51.13 B C ATOM 2220 CG LYS B 92 5.925 16.062 26.507 1.00 52.28 B C ATOM 2221 CD LYS B 92 5.457 16.428 25.111 1.00 56.69 B C ATOM 2222 CE LYS B 92 6.514 16.117 24.067 1.00 54.23 B C ATOM 2223 NZ LYS B 92 6.375 17.000 22.878 1.00 51.65 B N ATOM 2224 C LYS B 92 6.845 18.204 28.606 1.00 45.28 B C ATOM 2225 O LYS B 92 8.039 17.972 28.517 1.00 47.11 B O ATOM 2226 N ALA B 93 6.343 19.433 28.528 1.00 44.61 B N ATOM 2227 CA ALA B 93 7.201 20.602 28.418 1.00 42.10 B C ATOM 2228 CB ALA B 93 6.371 21.861 28.496 1.00 41.42 B C ATOM 2229 C ALA B 93 8.286 20.608 29.501 1.00 41.89 B C ATOM 2230 O ALA B 93 9.484 20.698 29.196 1.00 38.77 B O ATOM 2231 N MET B 94 7.860 20.519 30.762 1.00 43.36 B N ATOM 2232 CA MET B 94 8.781 20.508 31.903 1.00 40.24 B C ATOM 2233 CB MET B 94 8.014 20.483 33.226 1.00 41.12 B C ATOM 2234 CG MET B 94 7.304 21.792 33.572 1.00 44.34 B C ATOM 2235 SD MET B 94 6.190 21.619 34.992 1.00 42.55 B S ATOM 2236 CE MET B 94 5.646 23.308 35.253 1.00 40.03 B C ATOM 2237 C MET B 94 9.813 19.372 31.887 1.00 38.62 B C ATOM 2238 O MET B 94 10.893 19.521 32.451 1.00 39.23 B O ATOM 2239 N ARG B 95 9.481 18.247 31.261 1.00 40.53 B N ATOM 2240 CA ARG B 95 10.413 17.118 31.144 1.00 40.27 B C ATOM 2241 CB ARG B 95 9.673 15.801 30.880 1.00 43.17 B C ATOM 2242 CG ARG B 95 8.940 15.194 32.059 1.00 50.81 B C ATOM 2243 CD ARG B 95 8.274 13.896 31.627 1.00 50.30 B C ATOM 2244 NE ARG B 95 7.020 13.664 32.332 1.00 59.49 B N ATOM 2245 CZ ARG B 95 5.899 13.255 31.746 1.00 59.61 B C ATOM 2246 NH1 ARG B 95 5.874 13.023 30.437 1.00 57.56 B N ATOM 2247 NH2 ARG B 95 4.805 13.072 32.471 1.00 61.42 B N ATOM 2248 C ARG B 95 11.408 17.302 30.008 1.00 38.25 B C ATOM 2249 O ARG B 95 12.346 16.522 29.883 1.00 36.11 B O ATOM 2250 N THR B 96 11.192 18.305 29.161 1.00 36.88 B N ATOM 2251 CA THR B 96 12.015 18.445 27.957 1.00 37.14 B C ATOM 2252 CB THR B 96 11.305 19.267 26.886 1.00 35.78 B C ATOM 2253 OG1 THR B 96 9.949 18.827 26.798 1.00 40.76 B O ATOM 2254 CG2 THR B 96 11.968 19.067 25.534 1.00 38.38 B C ATOM 2255 C THR B 96 13.357 19.072 28.284 1.00 34.10 B C ATOM 2256 O THR B 96 13.415 20.161 28.872 1.00 33.78 B O ATOM 2257 N PRO B 97 14.444 18.373 27.928 1.00 34.31 B N ATOM 2258 CD PRO B 97 14.487 17.020 27.355 1.00 35.18 B C ATOM 2259 CA PRO B 97 15.783 18.947 28.072 1.00 33.33 B C ATOM 2260 CB PRO B 97 16.645 18.013 27.237 1.00 32.50 B C ATOM 2261 CG PRO B 97 15.964 16.704 27.367 1.00 38.80 B C ATOM 2262 C PRO B 97 15.788 20.358 27.504 1.00 31.56 B C ATOM 2263 O PRO B 97 15.038 20.643 26.571 1.00 28.23 B O ATOM 2264 N ARG B 98 16.603 21.235 28.077 1.00 31.15 B N ATOM 2265 CA ARG B 98 16.493 22.647 27.759 1.00 30.35 B C ATOM 2266 CB ARG B 98 15.224 23.217 28.382 1.00 27.02 B C ATOM 2267 CG ARG B 98 15.302 23.336 29.922 1.00 28.86 B C ATOM 2268 CD ARG B 98 14.234 24.293 30.464 1.00 29.57 B C ATOM 2269 NE ARG B 98 14.723 25.670 30.487 1.00 31.34 B N ATOM 2270 CZ ARG B 98 13.945 26.748 30.426 1.00 29.53 B C ATOM 2271 NH1 ARG B 98 12.635 26.614 30.334 1.00 27.65 B N ATOM 2272 NH2 ARG B 98 14.478 27.966 30.443 1.00 29.12 B N ATOM 2273 C ARG B 98 17.683 23.456 28.261 1.00 30.67 B C ATOM 2274 O ARG B 98 18.568 22.940 28.946 1.00 29.63 B O ATOM 2275 N CYS B 99 17.664 24.744 27.934 1.00 27.83 B N ATOM 2276 CA CYS B 99 18.707 25.665 28.341 1.00 27.69 B C ATOM 2277 CB CYS B 99 18.637 26.907 27.468 1.00 26.53 B C ATOM 2278 SG CYS B 99 19.786 28.177 27.936 1.00 25.26 B S ATOM 2279 C CYS B 99 18.566 26.044 29.823 1.00 29.26 B C ATOM 2280 O CYS B 99 17.451 26.169 30.329 1.00 28.86 B O ATOM 2281 N GLY B 100 19.701 26.223 30.505 1.00 28.11 B N ATOM 2282 CA GLY B 100 19.718 26.506 31.931 1.00 29.95 B C ATOM 2283 C GLY B 100 19.348 27.929 32.292 1.00 32.78 B C ATOM 2284 O GLY B 100 18.956 28.202 33.430 1.00 32.99 B O ATOM 2285 N VAL B 101 19.463 28.843 31.325 1.00 28.73 B N ATOM 2286 CA VAL B 101 19.168 30.254 31.569 1.00 29.95 B C ATOM 2287 CB VAL B 101 19.536 31.116 30.347 1.00 26.43 B C ATOM 2288 CG1 VAL B 101 19.136 32.585 30.560 1.00 23.85 B C ATOM 2289 CG2 VAL B 101 21.039 30.976 30.027 1.00 26.00 B C ATOM 2290 C VAL B 101 17.687 30.453 31.905 1.00 28.98 B C ATOM 2291 O VAL B 101 16.834 29.785 31.341 1.00 27.42 B O ATOM 2292 N PRO B 102 17.378 31.374 32.831 1.00 31.96 B N ATOM 2293 CA PRO B 102 15.965 31.518 33.222 1.00 34.34 B C ATOM 2294 C PRO B 102 15.104 32.146 32.124 1.00 35.79 B C ATOM 2295 CB PRO B 102 16.028 32.418 34.475 1.00 35.45 B C ATOM 2296 CG PRO B 102 17.413 32.192 35.036 1.00 35.25 B C ATOM 2297 CD PRO B 102 18.287 32.040 33.780 1.00 34.60 B C ATOM 2298 O PRO B 102 15.635 32.753 31.202 1.00 30.44 B O ATOM 2299 N ASP B 103 13.787 31.995 32.231 1.00 31.78 B N ATOM 2300 CA ASP B 103 12.867 32.577 31.258 1.00 35.82 B C ATOM 2301 C ASP B 103 12.401 33.944 31.736 1.00 37.44 B C ATOM 2302 CB ASP B 103 11.662 31.651 31.041 1.00 34.70 B C ATOM 2303 CG ASP B 103 12.073 30.279 30.558 1.00 33.62 B C ATOM 2304 OD1 ASP B 103 13.118 30.202 29.875 1.00 29.22 B O ATOM 2305 OD2 ASP B 103 11.370 29.281 30.841 1.00 29.60 B O ATOM 2306 O ASP B 103 12.142 34.842 30.935 1.00 34.45 B O ATOM 2307 N LEU B 104 12.305 34.095 33.055 1.00 39.78 B N ATOM 2308 CA LEU B 104 11.885 35.358 33.675 1.00 47.25 B C ATOM 2309 C LEU B 104 12.743 35.701 34.898 1.00 46.92 B C ATOM 2310 CB LEU B 104 10.416 35.278 34.094 1.00 46.98 B C ATOM 2311 CG LEU B 104 9.376 35.036 33.000 1.00 45.54 B C ATOM 2312 CD1 LEU B 104 8.016 34.802 33.640 1.00 49.06 B C ATOM 2313 CD2 LEU B 104 9.329 36.210 32.048 1.00 43.04 B C ATOM 2314 O LEU B 104 13.745 35.044 35.169 1.00 48.47 B O ATOM 2315 N GLY B 105 12.346 36.725 35.646 1.00 56.26 B N ATOM 2316 CA GLY B 105 13.111 37.132 36.815 1.00 62.60 B C ATOM 2317 C GLY B 105 12.274 37.397 38.056 1.00 61.85 B C ATOM 2318 O GLY B 105 11.059 37.541 37.947 1.00 64.62 B O ATOM 2319 N ARG B 106 12.887 37.443 39.241 1.00 64.34 B N ATOM 2320 CA ARG B 106 14.291 37.073 39.490 1.00 68.00 B C ATOM 2321 C ARG B 106 15.414 38.029 39.068 1.00 69.98 B C ATOM 2322 CB ARG B 106 14.599 35.656 38.997 1.00 64.01 B C ATOM 2323 CG ARG B 106 14.373 34.590 40.041 1.00 60.91 B C ATOM 2324 CD ARG B 106 14.361 33.228 39.411 1.00 58.01 B C ATOM 2325 NE ARG B 106 15.674 32.863 38.902 1.00 59.26 B N ATOM 2326 CZ ARG B 106 16.560 32.170 39.605 1.00 60.73 B C ATOM 2327 NH1 ARG B 106 16.251 31.772 40.837 1.00 59.87 B N ATOM 2328 NH2 ARG B 106 17.742 31.870 39.082 1.00 56.57 B N ATOM 2329 O ARG B 106 15.365 38.695 38.030 1.00 69.79 B O ATOM 2330 N PHE B 107 16.430 38.058 39.921 1.00 70.43 B N ATOM 2331 CA PHE B 107 17.674 38.755 39.669 1.00 67.30 B C ATOM 2332 C PHE B 107 18.686 37.751 39.194 1.00 65.37 B C ATOM 2333 CB PHE B 107 18.254 39.269 40.985 1.00 70.53 B C ATOM 2334 CG PHE B 107 17.720 40.591 41.421 1.00 73.01 B C ATOM 2335 CD1 PHE B 107 18.525 41.453 42.142 1.00 69.47 B C ATOM 2336 CD2 PHE B 107 16.424 40.975 41.124 1.00 74.54 B C ATOM 2337 CE1 PHE B 107 18.059 42.668 42.555 1.00 68.88 B C ATOM 2338 CE2 PHE B 107 15.946 42.202 41.537 1.00 72.52 B C ATOM 2339 CZ PHE B 107 16.767 43.050 42.256 1.00 72.60 B C ATOM 2340 O PHE B 107 18.511 36.548 39.362 1.00 65.58 B O ATOM 2341 N GLN B 108 19.727 38.286 38.572 1.00 67.17 B N ATOM 2342 CA GLN B 108 21.110 37.858 38.747 1.00 59.93 B C ATOM 2343 C GLN B 108 21.775 39.113 38.266 1.00 57.96 B C ATOM 2344 CB GLN B 108 21.515 36.672 37.875 1.00 56.10 B C ATOM 2345 CG GLN B 108 21.024 35.331 38.391 1.00 57.59 B C ATOM 2346 CD GLN B 108 19.635 34.986 37.875 1.00 62.64 B C ATOM 2347 OE1 GLN B 108 19.184 35.519 36.846 1.00 60.16 B O ATOM 2348 NE2 GLN B 108 18.942 34.102 38.593 1.00 55.66 B N ATOM 2349 O GLN B 108 22.091 39.234 37.082 1.00 61.09 B O ATOM 2350 N VAL B 109 21.905 40.087 39.159 1.00 57.62 B N ATOM 2351 CA VAL B 109 22.386 41.387 38.734 1.00 57.73 B C ATOM 2352 C VAL B 109 23.626 41.185 37.866 1.00 54.43 B C ATOM 2353 CB VAL B 109 22.653 42.349 39.916 1.00 57.85 B C ATOM 2354 CG1 VAL B 109 24.142 42.696 40.012 1.00 56.19 B C ATOM 2355 CG2 VAL B 109 22.103 41.772 41.229 1.00 60.46 B C ATOM 2356 O VAL B 109 24.575 40.490 38.246 1.00 50.27 B O ATOM 2357 N PHE B 110 23.568 41.743 36.667 1.00 51.11 B N ATOM 2358 CA PHE B 110 24.698 41.701 35.758 1.00 47.89 B C ATOM 2359 C PHE B 110 25.233 43.096 35.582 1.00 45.68 B C ATOM 2360 CB PHE B 110 24.305 41.089 34.413 1.00 41.35 B C ATOM 2361 CG PHE B 110 24.221 39.602 34.451 1.00 42.00 B C ATOM 2362 CD1 PHE B 110 23.023 38.955 34.211 1.00 42.08 B C ATOM 2363 CD2 PHE B 110 25.342 38.848 34.767 1.00 41.87 B C ATOM 2364 CE1 PHE B 110 22.942 37.576 34.269 1.00 41.08 B C ATOM 2365 CE2 PHE B 110 25.278 37.468 34.819 1.00 41.35 B C ATOM 2366 CZ PHE B 110 24.067 36.830 34.578 1.00 40.11 B C ATOM 2367 O PHE B 110 24.529 44.079 35.802 1.00 49.71 B O ATOM 2368 N GLU B 111 26.490 43.184 35.193 1.00 44.15 B N ATOM 2369 CA GLU B 111 27.118 44.476 35.068 1.00 42.39 B C ATOM 2370 CB GLU B 111 28.595 44.364 35.423 1.00 45.58 B C ATOM 2371 CG GLU B 111 29.372 45.650 35.302 1.00 54.45 B C ATOM 2372 CD GLU B 111 30.736 45.542 35.948 1.00 61.76 B C ATOM 2373 OE1 GLU B 111 30.987 44.510 36.615 1.00 64.13 B O ATOM 2374 OE2 GLU B 111 31.546 46.483 35.798 1.00 64.21 B O ATOM 2375 C GLU B 111 26.938 45.027 33.665 1.00 45.59 B C ATOM 2376 O GLU B 111 27.110 44.317 32.674 1.00 41.99 B O ATOM 2377 N GLY B 112 26.568 46.298 33.592 1.00 44.08 B N ATOM 2378 CA GLY B 112 26.615 47.031 32.346 1.00 36.40 B C ATOM 2379 C GLY B 112 25.395 46.886 31.464 1.00 41.12 B C ATOM 2380 O GLY B 112 24.319 46.502 31.903 1.00 38.89 B O ATOM 2381 N ASP B 113 25.613 47.183 30.191 1.00 39.05 B N ATOM 2382 CA ASP B 113 24.588 47.286 29.167 1.00 42.01 B C ATOM 2383 CB ASP B 113 25.272 47.851 27.926 1.00 38.42 B C ATOM 2384 CG ASP B 113 24.418 48.805 27.207 1.00 39.78 B C ATOM 2385 OD1 ASP B 113 23.389 49.203 27.790 1.00 45.34 B O ATOM 2386 OD2 ASP B 113 24.765 49.152 26.070 1.00 41.96 B O ATOM 2387 C ASP B 113 23.895 45.975 28.757 1.00 37.89 B C ATOM 2388 O ASP B 113 22.781 45.984 28.224 1.00 33.57 B O ATOM 2389 N LEU B 114 24.590 44.865 28.961 1.00 32.28 B N ATOM 2390 CA LEU B 114 24.180 43.572 28.427 1.00 35.12 B C ATOM 2391 CB LEU B 114 22.798 43.150 28.948 1.00 33.15 B C ATOM 2392 CG LEU B 114 22.605 43.190 30.469 1.00 38.09 B C ATOM 2393 CD1 LEU B 114 21.431 42.276 30.879 1.00 37.51 B C ATOM 2394 CD2 LEU B 114 23.880 42.812 31.215 1.00 34.18 B C ATOM 2395 C LEU B 114 24.236 43.511 26.893 1.00 33.88 B C ATOM 2396 O LEU B 114 23.598 42.658 26.288 1.00 34.87 B O ATOM 2397 N LYS B 115 25.001 44.423 26.284 1.00 37.42 B N ATOM 2398 CA LYS B 115 25.389 44.342 24.871 1.00 35.10 B C ATOM 2399 CB LYS B 115 24.737 45.455 24.043 1.00 37.98 B C ATOM 2400 CG LYS B 115 23.245 45.293 23.859 1.00 40.88 B C ATOM 2401 CD LYS B 115 22.741 46.117 22.691 1.00 43.17 B C ATOM 2402 CE LYS B 115 22.973 47.609 22.880 1.00 46.08 B C ATOM 2403 NZ LYS B 115 21.908 48.379 22.139 1.00 48.01 B N ATOM 2404 C LYS B 115 26.899 44.498 24.758 1.00 36.32 B C ATOM 2405 O LYS B 115 27.529 45.033 25.682 1.00 32.62 B O ATOM 2406 N TRP B 116 27.475 44.033 23.643 1.00 28.18 B N ATOM 2407 CA TRP B 116 28.880 44.311 23.346 1.00 29.82 B C ATOM 2408 CB TRP B 116 29.487 43.276 22.386 1.00 29.96 B C ATOM 2409 CG TRP B 116 29.522 41.888 22.923 1.00 26.83 B C ATOM 2410 CD2 TRP B 116 30.284 41.413 24.038 1.00 30.05 B C ATOM 2411 CE2 TRP B 116 30.002 40.039 24.180 1.00 31.33 B C ATOM 2412 CE3 TRP B 116 31.182 42.013 24.925 1.00 30.16 B C ATOM 2413 CD1 TRP B 116 28.832 40.810 22.442 1.00 29.79 B C ATOM 2414 NE1 TRP B 116 29.123 39.697 23.186 1.00 33.82 B N ATOM 2415 CZ2 TRP B 116 30.572 39.256 25.184 1.00 27.66 B C ATOM 2416 CZ3 TRP B 116 31.755 41.229 25.915 1.00 33.01 B C ATOM 2417 CH2 TRP B 116 31.447 39.866 26.034 1.00 32.26 B C ATOM 2418 C TRP B 116 29.029 45.691 22.720 1.00 34.26 B C ATOM 2419 O TRP B 116 28.147 46.155 21.991 1.00 32.27 B O ATOM 2420 N HIS B 117 30.168 46.326 22.973 1.00 35.09 B N ATOM 2421 CA HIS B 117 30.416 47.673 22.467 1.00 33.70 B C ATOM 2422 CB HIS B 117 30.415 48.670 23.615 1.00 31.37 B C ATOM 2423 CG HIS B 117 29.103 48.735 24.315 1.00 36.76 B C ATOM 2424 CD2 HIS B 117 28.652 48.106 25.422 1.00 35.38 B C ATOM 2425 ND1 HIS B 117 28.047 49.480 23.835 1.00 39.73 B N ATOM 2426 CE1 HIS B 117 27.007 49.329 24.635 1.00 38.20 B C ATOM 2427 NE2 HIS B 117 27.348 48.500 25.608 1.00 42.19 B N ATOM 2428 C HIS B 117 31.689 47.787 21.649 1.00 35.31 B C ATOM 2429 O HIS B 117 32.334 48.834 21.623 1.00 35.80 B O ATOM 2430 N HIS B 118 32.034 46.685 20.992 1.00 34.07 B N ATOM 2431 CA HIS B 118 33.114 46.633 20.026 1.00 34.15 B C ATOM 2432 CB HIS B 118 34.450 46.389 20.724 1.00 36.66 B C ATOM 2433 CG HIS B 118 34.565 45.050 21.382 1.00 34.47 B C ATOM 2434 CD2 HIS B 118 35.045 43.868 20.922 1.00 35.49 B C ATOM 2435 ND1 HIS B 118 34.190 44.829 22.691 1.00 31.81 B N ATOM 2436 CE1 HIS B 118 34.426 43.565 23.007 1.00 33.82 B C ATOM 2437 NE2 HIS B 118 34.947 42.962 21.954 1.00 33.20 B N ATOM 2438 C HIS B 118 32.762 45.504 19.064 1.00 33.10 B C ATOM 2439 O HIS B 118 32.016 44.602 19.425 1.00 32.47 B O ATOM 2440 N HIS B 119 33.269 45.543 17.842 1.00 32.23 B N ATOM 2441 CA HIS B 119 32.701 44.661 16.820 1.00 34.01 B C ATOM 2442 CB HIS B 119 32.573 45.379 15.477 1.00 38.72 B C ATOM 2443 CG HIS B 119 33.697 45.095 14.535 1.00 42.44 B C ATOM 2444 CD2 HIS B 119 33.760 44.310 13.429 1.00 43.84 B C ATOM 2445 ND1 HIS B 119 34.948 45.661 14.675 1.00 45.99 B N ATOM 2446 CE1 HIS B 119 35.730 45.232 13.701 1.00 47.41 B C ATOM 2447 NE2 HIS B 119 35.037 44.412 12.932 1.00 42.40 B N ATOM 2448 C HIS B 119 33.401 43.318 16.639 1.00 33.32 B C ATOM 2449 O HIS B 119 32.782 42.351 16.187 1.00 30.35 B O ATOM 2450 N ASN B 120 34.686 43.249 16.964 1.00 35.94 B N ATOM 2451 CA ASN B 120 35.372 41.973 16.855 1.00 34.45 B C ATOM 2452 CB ASN B 120 36.817 42.122 16.408 1.00 37.17 B C ATOM 2453 CG ASN B 120 37.501 40.763 16.180 1.00 42.30 B C ATOM 2454 OD1 ASN B 120 36.856 39.763 15.812 1.00 33.27 B O ATOM 2455 ND2 ASN B 120 38.815 40.727 16.396 1.00 42.16 B N ATOM 2456 C ASN B 120 35.308 41.216 18.167 1.00 34.97 B C ATOM 2457 O ASN B 120 36.062 41.488 19.096 1.00 31.76 B O ATOM 2458 N ILE B 121 34.408 40.246 18.224 1.00 31.32 B N ATOM 2459 CA ILE B 121 34.237 39.473 19.437 1.00 31.99 B C ATOM 2460 CB ILE B 121 32.798 39.030 19.602 1.00 26.89 B C ATOM 2461 CG2 ILE B 121 32.600 38.432 20.970 1.00 26.28 B C ATOM 2462 CG1 ILE B 121 31.871 40.219 19.363 1.00 30.44 B C ATOM 2463 CD1 ILE B 121 32.062 41.359 20.353 1.00 30.61 B C ATOM 2464 C ILE B 121 35.157 38.277 19.388 1.00 30.91 B C ATOM 2465 O ILE B 121 35.188 37.551 18.395 1.00 31.79 B O ATOM 2466 N THR B 122 35.928 38.096 20.451 1.00 28.28 B N ATOM 2467 CA THR B 122 36.887 37.008 20.510 1.00 27.84 B C ATOM 2468 CB THR B 122 38.238 37.487 21.040 1.00 29.87 B C ATOM 2469 OG1 THR B 122 38.073 37.969 22.380 1.00 29.34 B O ATOM 2470 CG2 THR B 122 38.796 38.606 20.159 1.00 27.39 B C ATOM 2471 C THR B 122 36.379 35.926 21.436 1.00 29.16 B C ATOM 2472 O THR B 122 35.688 36.203 22.424 1.00 26.04 B O ATOM 2473 N TYR B 123 36.740 34.686 21.136 1.00 28.30 B N ATOM 2474 CA TYR B 123 36.300 33.577 21.966 1.00 28.28 B C ATOM 2475 CB TYR B 123 35.039 32.936 21.394 1.00 28.24 B C ATOM 2476 CG TYR B 123 35.183 32.226 20.054 1.00 28.94 B C ATOM 2477 CD1 TYR B 123 35.043 32.914 18.856 1.00 25.71 B C ATOM 2478 CE1 TYR B 123 35.141 32.252 17.634 1.00 26.95 B C ATOM 2479 CD2 TYR B 123 35.432 30.854 20.000 1.00 29.89 B C ATOM 2480 CE2 TYR B 123 35.539 30.187 18.800 1.00 24.71 B C ATOM 2481 CZ TYR B 123 35.395 30.892 17.625 1.00 29.20 B C ATOM 2482 OH TYR B 123 35.486 30.213 16.446 1.00 29.90 B O ATOM 2483 C TYR B 123 37.381 32.535 22.163 1.00 28.54 B C ATOM 2484 O TYR B 123 38.149 32.250 21.253 1.00 27.88 B O ATOM 2485 N TRP B 124 37.429 31.971 23.365 1.00 31.22 B N ATOM 2486 CA TRP B 124 38.419 30.973 23.702 1.00 28.09 B C ATOM 2487 CB TRP B 124 39.264 31.460 24.882 1.00 31.90 B C ATOM 2488 CG TRP B 124 40.312 30.498 25.331 1.00 32.37 B C ATOM 2489 CD2 TRP B 124 40.767 30.287 26.674 1.00 37.67 B C ATOM 2490 CE2 TRP B 124 41.780 29.301 26.623 1.00 34.69 B C ATOM 2491 CE3 TRP B 124 40.418 30.831 27.916 1.00 36.22 B C ATOM 2492 CD1 TRP B 124 41.049 29.658 24.541 1.00 36.33 B C ATOM 2493 NE1 TRP B 124 41.929 28.932 25.312 1.00 37.02 B N ATOM 2494 CZ2 TRP B 124 42.443 28.854 27.760 1.00 36.24 B C ATOM 2495 CZ3 TRP B 124 41.079 30.384 29.043 1.00 38.16 B C ATOM 2496 CH2 TRP B 124 42.081 29.407 28.958 1.00 38.34 B C ATOM 2497 C TRP B 124 37.751 29.660 24.059 1.00 32.28 B C ATOM 2498 O TRP B 124 36.956 29.585 24.997 1.00 33.08 B O ATOM 2499 N ILE B 125 38.075 28.620 23.308 1.00 31.43 B N ATOM 2500 CA ILE B 125 37.652 27.288 23.686 1.00 31.79 B C ATOM 2501 CB ILE B 125 37.652 26.334 22.490 1.00 36.01 B C ATOM 2502 CG2 ILE B 125 37.029 25.016 22.887 1.00 35.00 B C ATOM 2503 CG1 ILE B 125 36.928 26.987 21.304 1.00 35.74 B C ATOM 2504 CD1 ILE B 125 36.826 26.127 20.068 1.00 30.71 B C ATOM 2505 C ILE B 125 38.607 26.813 24.771 1.00 34.87 B C ATOM 2506 O ILE B 125 39.768 26.518 24.515 1.00 35.69 B O ATOM 2507 N GLN B 126 38.115 26.782 25.996 1.00 33.98 B N ATOM 2508 CA GLN B 126 38.959 26.609 27.167 1.00 37.38 B C ATOM 2509 CB GLN B 126 38.274 27.289 28.361 1.00 37.02 B C ATOM 2510 CG GLN B 126 38.952 27.162 29.700 1.00 41.93 B C ATOM 2511 CD GLN B 126 38.232 27.964 30.770 1.00 41.63 B C ATOM 2512 OE1 GLN B 126 37.202 27.536 31.306 1.00 41.92 B O ATOM 2513 NE2 GLN B 126 38.770 29.137 31.083 1.00 43.54 B N ATOM 2514 C GLN B 126 39.237 25.125 27.421 1.00 37.09 B C ATOM 2515 O GLN B 126 40.247 24.772 28.021 1.00 40.10 B O ATOM 2516 N ASN B 127 38.339 24.259 26.958 1.00 37.26 B N ATOM 2517 CA ASN B 127 38.549 22.809 27.027 1.00 32.95 B C ATOM 2518 CB ASN B 127 38.472 22.291 28.472 1.00 36.15 B C ATOM 2519 CG ASN B 127 37.059 22.302 29.034 1.00 36.13 B C ATOM 2520 OD1 ASN B 127 36.209 23.060 28.589 1.00 34.82 B O ATOM 2521 ND2 ASN B 127 36.808 21.448 30.020 1.00 35.31 B N ATOM 2522 C ASN B 127 37.614 22.050 26.073 1.00 36.87 B C ATOM 2523 O ASN B 127 36.801 22.676 25.381 1.00 36.09 B O ATOM 2524 N TYR B 128 37.739 20.720 26.014 1.00 34.17 B N ATOM 2525 CA TYR B 128 37.004 19.921 25.031 1.00 30.92 B C ATOM 2526 CB TYR B 128 37.945 19.435 23.934 1.00 34.44 B C ATOM 2527 CG TYR B 128 38.473 20.504 23.041 1.00 35.03 B C ATOM 2528 CD1 TYR B 128 37.872 20.760 21.826 1.00 33.74 B C ATOM 2529 CE1 TYR B 128 38.356 21.727 20.990 1.00 33.23 B C ATOM 2530 CD2 TYR B 128 39.589 21.250 23.400 1.00 36.71 B C ATOM 2531 CE2 TYR B 128 40.081 22.231 22.564 1.00 36.37 B C ATOM 2532 CZ TYR B 128 39.456 22.459 21.357 1.00 35.71 B C ATOM 2533 OH TYR B 128 39.929 23.427 20.498 1.00 37.79 B O ATOM 2534 C TYR B 128 36.360 18.678 25.588 1.00 34.96 B C ATOM 2535 O TYR B 128 37.002 17.916 26.302 1.00 41.28 B O ATOM 2536 N SER B 129 35.111 18.440 25.209 1.00 30.87 B N ATOM 2537 CA SER B 129 34.449 17.185 25.529 1.00 33.97 B C ATOM 2538 CB SER B 129 32.953 17.263 25.218 1.00 31.60 B C ATOM 2539 OG SER B 129 32.406 15.967 25.067 1.00 32.67 B O ATOM 2540 C SER B 129 35.084 16.038 24.750 1.00 37.85 B C ATOM 2541 O SER B 129 35.600 16.231 23.644 1.00 39.17 B O ATOM 2542 N GLU B 130 35.030 14.840 25.318 1.00 37.05 B N ATOM 2543 CA GLU B 130 35.640 13.674 24.689 1.00 36.25 B C ATOM 2544 CB GLU B 130 36.103 12.676 25.750 1.00 38.16 B C ATOM 2545 CG GLU B 130 37.297 13.165 26.536 1.00 43.44 B C ATOM 2546 CD GLU B 130 38.477 13.517 25.632 1.00 53.48 B C ATOM 2547 OE1 GLU B 130 38.849 12.670 24.785 1.00 55.72 B O ATOM 2548 OE2 GLU B 130 39.029 14.641 25.759 1.00 56.89 B O ATOM 2549 C GLU B 130 34.716 12.985 23.702 1.00 37.68 B C ATOM 2550 O GLU B 130 35.088 11.979 23.093 1.00 40.60 B O ATOM 2551 N ASP B 131 33.511 13.515 23.541 1.00 34.46 B N ATOM 2552 CA ASP B 131 32.526 12.858 22.697 1.00 35.34 B C ATOM 2553 CB ASP B 131 31.124 13.308 23.069 1.00 34.35 B C ATOM 2554 CG ASP B 131 30.834 13.135 24.540 1.00 37.96 B C ATOM 2555 OD1 ASP B 131 31.581 12.391 25.223 1.00 37.43 B O ATOM 2556 OD2 ASP B 131 29.856 13.754 25.007 1.00 36.10 B O ATOM 2557 C ASP B 131 32.747 13.093 21.207 1.00 34.52 B C ATOM 2558 O ASP B 131 32.189 12.367 20.385 1.00 32.42 B O ATOM 2559 N LEU B 132 33.544 14.107 20.872 1.00 34.53 B N ATOM 2560 CA LEU B 132 33.798 14.496 19.484 1.00 31.14 B C ATOM 2561 CB LEU B 132 32.890 15.676 19.085 1.00 32.96 B C ATOM 2562 CG LEU B 132 31.383 15.412 18.953 1.00 33.73 B C ATOM 2563 CD1 LEU B 132 30.544 16.680 19.076 1.00 27.93 B C ATOM 2564 CD2 LEU B 132 31.112 14.705 17.621 1.00 31.04 B C ATOM 2565 C LEU B 132 35.252 14.895 19.266 1.00 32.34 B C ATOM 2566 O LEU B 132 35.893 15.446 20.167 1.00 34.88 B O ATOM 2567 N PRO B 133 35.776 14.646 18.054 1.00 32.97 B N ATOM 2568 CD PRO B 133 35.129 13.947 16.930 1.00 30.43 B C ATOM 2569 CA PRO B 133 37.109 15.142 17.707 1.00 30.83 B C ATOM 2570 CB PRO B 133 37.170 14.937 16.190 1.00 29.25 B C ATOM 2571 CG PRO B 133 36.244 13.803 15.920 1.00 28.79 B C ATOM 2572 C PRO B 133 37.179 16.629 18.022 1.00 33.06 B C ATOM 2573 O PRO B 133 36.149 17.300 17.954 1.00 32.75 B O ATOM 2574 N ARG B 134 38.361 17.138 18.349 1.00 30.39 B N ATOM 2575 CA ARG B 134 38.512 18.561 18.605 1.00 31.73 B C ATOM 2576 CB ARG B 134 39.927 18.889 19.077 1.00 35.29 B C ATOM 2577 CG ARG B 134 40.282 18.233 20.392 1.00 37.20 B C ATOM 2578 CD ARG B 134 41.492 18.895 21.019 1.00 42.64 B C ATOM 2579 NE ARG B 134 41.608 18.524 22.425 1.00 46.65 B N ATOM 2580 CZ ARG B 134 42.493 19.037 23.271 1.00 48.63 B C ATOM 2581 NH1 ARG B 134 43.360 19.955 22.855 1.00 46.45 B N ATOM 2582 NH2 ARG B 134 42.509 18.630 24.541 1.00 47.56 B N ATOM 2583 C ARG B 134 38.162 19.405 17.394 1.00 33.90 B C ATOM 2584 O ARG B 134 37.568 20.476 17.535 1.00 34.24 B O ATOM 2585 N ALA B 135 38.535 18.930 16.207 1.00 31.53 B N ATOM 2586 CA ALA B 135 38.304 19.691 14.984 1.00 33.19 B C ATOM 2587 CB ALA B 135 38.973 19.007 13.782 1.00 28.43 B C ATOM 2588 C ALA B 135 36.809 19.859 14.735 1.00 32.71 B C ATOM 2589 O ALA B 135 36.359 20.893 14.236 1.00 34.13 B O ATOM 2590 N VAL B 136 36.045 18.827 15.075 1.00 33.83 B N ATOM 2591 CA VAL B 136 34.599 18.857 14.897 1.00 30.82 B C ATOM 2592 CB VAL B 136 33.979 17.456 15.052 1.00 31.74 B C ATOM 2593 CG1 VAL B 136 32.494 17.510 14.789 1.00 31.08 B C ATOM 2594 CG2 VAL B 136 34.631 16.484 14.088 1.00 32.80 B C ATOM 2595 C VAL B 136 33.967 19.844 15.890 1.00 27.26 B C ATOM 2596 O VAL B 136 33.031 20.577 15.551 1.00 28.06 B O ATOM 2597 N ILE B 137 34.494 19.864 17.109 1.00 27.08 B N ATOM 2598 CA ILE B 137 34.052 20.816 18.123 1.00 26.33 B C ATOM 2599 CB ILE B 137 34.680 20.513 19.499 1.00 28.51 B C ATOM 2600 CG2 ILE B 137 34.515 21.715 20.431 1.00 30.04 B C ATOM 2601 CG1 ILE B 137 34.035 19.251 20.107 1.00 32.07 B C ATOM 2602 CD1 ILE B 137 34.739 18.692 21.351 1.00 29.01 B C ATOM 2603 C ILE B 137 34.356 22.253 17.677 1.00 27.46 B C ATOM 2604 O ILE B 137 33.450 23.090 17.586 1.00 29.77 B O ATOM 2605 N ASP B 138 35.623 22.525 17.390 1.00 24.64 B N ATOM 2606 CA ASP B 138 36.045 23.787 16.790 1.00 28.63 B C ATOM 2607 CB ASP B 138 37.464 23.659 16.227 1.00 27.81 B C ATOM 2608 CG ASP B 138 38.513 23.510 17.313 1.00 36.90 B C ATOM 2609 OD1 ASP B 138 38.142 23.617 18.511 1.00 33.26 B O ATOM 2610 OD2 ASP B 138 39.707 23.290 16.968 1.00 33.17 B O ATOM 2611 C ASP B 138 35.117 24.218 15.658 1.00 26.40 B C ATOM 2612 O ASP B 138 34.696 25.364 15.576 1.00 27.46 B O ATOM 2613 N ASP B 139 34.817 23.289 14.766 1.00 27.90 B N ATOM 2614 CA ASP B 139 34.027 23.623 13.602 1.00 27.65 B C ATOM 2615 CB ASP B 139 34.138 22.519 12.556 1.00 30.62 B C ATOM 2616 CG ASP B 139 33.228 22.758 11.374 1.00 32.90 B C ATOM 2617 OD1 ASP B 139 33.567 23.594 10.510 1.00 34.57 B O ATOM 2618 OD2 ASP B 139 32.163 22.115 11.322 1.00 31.46 B O ATOM 2619 C ASP B 139 32.570 23.868 13.969 1.00 27.13 B C ATOM 2620 O ASP B 139 31.918 24.722 13.380 1.00 25.46 B O ATOM 2621 N ALA B 140 32.057 23.130 14.955 1.00 26.68 B N ATOM 2622 CA ALA B 140 30.689 23.377 15.434 1.00 26.01 B C ATOM 2623 CB ALA B 140 30.262 22.319 16.461 1.00 20.34 B C ATOM 2624 C ALA B 140 30.544 24.785 16.017 1.00 25.12 B C ATOM 2625 O ALA B 140 29.569 25.498 15.749 1.00 20.71 B O ATOM 2626 N PHE B 141 31.498 25.179 16.846 1.00 25.84 B N ATOM 2627 CA PHE B 141 31.434 26.518 17.420 1.00 25.66 B C ATOM 2628 CB PHE B 141 32.465 26.715 18.535 1.00 22.52 B C ATOM 2629 CG PHE B 141 32.263 25.836 19.734 1.00 27.19 B C ATOM 2630 CD1 PHE B 141 31.002 25.543 20.203 1.00 26.26 B C ATOM 2631 CD2 PHE B 141 33.353 25.325 20.411 1.00 24.11 B C ATOM 2632 CE1 PHE B 141 30.841 24.737 21.324 1.00 30.27 B C ATOM 2633 CE2 PHE B 141 33.202 24.532 21.510 1.00 27.64 B C ATOM 2634 CZ PHE B 141 31.956 24.228 21.977 1.00 24.85 B C ATOM 2635 C PHE B 141 31.614 27.588 16.316 1.00 24.97 B C ATOM 2636 O PHE B 141 30.932 28.601 16.330 1.00 26.56 B O ATOM 2637 N ALA B 142 32.529 27.378 15.366 1.00 25.52 B N ATOM 2638 CA ALA B 142 32.709 28.385 14.309 1.00 25.90 B C ATOM 2639 CB ALA B 142 33.884 28.018 13.384 1.00 27.24 B C ATOM 2640 C ALA B 142 31.429 28.578 13.487 1.00 26.71 B C ATOM 2641 O ALA B 142 31.058 29.691 13.127 1.00 23.88 B O ATOM 2642 N ARG B 143 30.772 27.468 13.178 1.00 27.10 B N ATOM 2643 CA ARG B 143 29.542 27.488 12.397 1.00 25.43 B C ATOM 2644 CB ARG B 143 29.134 26.060 12.047 1.00 26.35 B C ATOM 2645 CG ARG B 143 30.161 25.370 11.124 1.00 26.97 B C ATOM 2646 CD ARG B 143 30.068 23.848 11.280 1.00 33.61 B C ATOM 2647 NE ARG B 143 28.716 23.469 10.975 1.00 34.98 B N ATOM 2648 CZ ARG B 143 28.004 22.534 11.575 1.00 27.34 B C ATOM 2649 NH1 ARG B 143 28.494 21.757 12.538 1.00 28.40 B N ATOM 2650 NH2 ARG B 143 26.768 22.373 11.155 1.00 30.14 B N ATOM 2651 C ARG B 143 28.427 28.189 13.161 1.00 26.18 B C ATOM 2652 O ARG B 143 27.677 28.989 12.604 1.00 24.56 B O ATOM 2653 N ALA B 144 28.319 27.898 14.450 1.00 23.96 B N ATOM 2654 CA ALA B 144 27.351 28.615 15.261 1.00 24.95 B C ATOM 2655 CB ALA B 144 27.309 28.050 16.690 1.00 23.20 B C ATOM 2656 C ALA B 144 27.593 30.136 15.255 1.00 22.91 B C ATOM 2657 O ALA B 144 26.644 30.911 15.173 1.00 21.81 B O ATOM 2658 N PHE B 145 28.849 30.573 15.332 1.00 22.75 B N ATOM 2659 CA PHE B 145 29.124 32.012 15.243 1.00 24.22 B C ATOM 2660 CB PHE B 145 30.582 32.328 15.596 1.00 22.90 B C ATOM 2661 CG PHE B 145 30.859 32.342 17.076 1.00 22.99 B C ATOM 2662 CD1 PHE B 145 30.178 33.217 17.920 1.00 26.40 B C ATOM 2663 CD2 PHE B 145 31.777 31.465 17.634 1.00 23.15 B C ATOM 2664 CE1 PHE B 145 30.428 33.222 19.304 1.00 22.82 B C ATOM 2665 CE2 PHE B 145 32.032 31.472 19.001 1.00 24.46 B C ATOM 2666 CZ PHE B 145 31.349 32.353 19.833 1.00 22.76 B C ATOM 2667 C PHE B 145 28.776 32.590 13.864 1.00 28.53 B C ATOM 2668 O PHE B 145 28.271 33.716 13.744 1.00 25.58 B O ATOM 2669 N ALA B 146 29.063 31.830 12.807 1.00 28.95 B N ATOM 2670 CA ALA B 146 28.777 32.325 11.460 1.00 25.57 B C ATOM 2671 CB ALA B 146 29.259 31.347 10.400 1.00 26.71 B C ATOM 2672 C ALA B 146 27.299 32.625 11.276 1.00 24.70 B C ATOM 2673 O ALA B 146 26.943 33.476 10.457 1.00 26.26 B O ATOM 2674 N LEU B 147 26.430 31.929 12.012 1.00 26.21 B N ATOM 2675 CA LEU B 147 24.997 32.236 11.945 1.00 23.60 B C ATOM 2676 CB LEU B 147 24.157 31.335 12.859 1.00 25.21 B C ATOM 2677 CG LEU B 147 23.940 29.861 12.560 1.00 25.66 B C ATOM 2678 CD1 LEU B 147 23.246 29.167 13.762 1.00 23.23 B C ATOM 2679 CD2 LEU B 147 23.132 29.692 11.275 1.00 24.27 B C ATOM 2680 C LEU B 147 24.787 33.679 12.382 1.00 26.09 B C ATOM 2681 O LEU B 147 24.070 34.452 11.738 1.00 24.52 B O ATOM 2682 N TRP B 148 25.407 34.039 13.496 1.00 22.61 B N ATOM 2683 CA TRP B 148 25.198 35.363 14.057 1.00 24.85 B C ATOM 2684 CB TRP B 148 25.552 35.358 15.547 1.00 24.53 B C ATOM 2685 CG TRP B 148 24.604 34.494 16.333 1.00 22.25 B C ATOM 2686 CD2 TRP B 148 23.202 34.728 16.543 1.00 25.90 B C ATOM 2687 CE2 TRP B 148 22.711 33.662 17.328 1.00 26.23 B C ATOM 2688 CE3 TRP B 148 22.314 35.740 16.164 1.00 22.79 B C ATOM 2689 CD1 TRP B 148 24.895 33.311 16.965 1.00 24.08 B C ATOM 2690 NE1 TRP B 148 23.764 32.810 17.566 1.00 21.99 B N ATOM 2691 CZ2 TRP B 148 21.373 33.582 17.738 1.00 24.20 B C ATOM 2692 CZ3 TRP B 148 20.983 35.655 16.562 1.00 25.88 B C ATOM 2693 CH2 TRP B 148 20.526 34.583 17.332 1.00 22.01 B C ATOM 2694 C TRP B 148 25.975 36.427 13.305 1.00 25.10 B C ATOM 2695 O TRP B 148 25.538 37.570 13.199 1.00 25.33 B O ATOM 2696 N SER B 149 27.125 36.038 12.765 1.00 23.03 B N ATOM 2697 CA SER B 149 27.979 36.965 12.045 1.00 23.74 B C ATOM 2698 CB SER B 149 29.180 36.204 11.470 1.00 25.15 B C ATOM 2699 OG SER B 149 30.216 37.096 11.161 1.00 31.30 B O ATOM 2700 C SER B 149 27.215 37.598 10.893 1.00 24.77 B C ATOM 2701 O SER B 149 27.318 38.794 10.632 1.00 24.27 B O ATOM 2702 N ALA B 150 26.466 36.775 10.176 1.00 21.84 B N ATOM 2703 CA ALA B 150 25.823 37.239 8.954 1.00 24.59 B C ATOM 2704 CB ALA B 150 25.260 36.067 8.161 1.00 22.47 B C ATOM 2705 C ALA B 150 24.739 38.286 9.202 1.00 24.53 B C ATOM 2706 O ALA B 150 24.445 39.073 8.310 1.00 23.31 B O ATOM 2707 N VAL B 151 24.151 38.295 10.407 1.00 23.53 B N ATOM 2708 CA VAL B 151 22.973 39.132 10.682 1.00 25.98 B C ATOM 2709 CB VAL B 151 21.795 38.299 11.231 1.00 29.35 B C ATOM 2710 CG1 VAL B 151 21.184 37.409 10.129 1.00 21.18 B C ATOM 2711 CG2 VAL B 151 22.256 37.462 12.436 1.00 26.13 B C ATOM 2712 C VAL B 151 23.251 40.261 11.675 1.00 28.03 B C ATOM 2713 O VAL B 151 22.325 40.871 12.181 1.00 25.95 B O ATOM 2714 N THR B 152 24.526 40.522 11.954 1.00 28.10 B N ATOM 2715 CA THR B 152 24.916 41.578 12.883 1.00 27.38 B C ATOM 2716 CB THR B 152 25.350 41.002 14.222 1.00 27.21 B C ATOM 2717 OG1 THR B 152 26.576 40.292 14.036 1.00 28.58 B O ATOM 2718 CG2 THR B 152 24.291 40.053 14.785 1.00 27.38 B C ATOM 2719 C THR B 152 26.167 42.242 12.332 1.00 29.69 B C ATOM 2720 O THR B 152 26.803 41.696 11.436 1.00 29.80 B O ATOM 2721 N PRO B 153 26.523 43.414 12.876 1.00 28.16 B N ATOM 2722 CD PRO B 153 25.662 44.244 13.735 1.00 29.79 B C ATOM 2723 CA PRO B 153 27.788 44.087 12.577 1.00 31.90 B C ATOM 2724 CB PRO B 153 27.545 45.528 13.066 1.00 29.62 B C ATOM 2725 CG PRO B 153 26.072 45.616 13.352 1.00 32.20 B C ATOM 2726 C PRO B 153 28.961 43.482 13.349 1.00 31.33 B C ATOM 2727 O PRO B 153 29.987 44.136 13.526 1.00 33.17 B O ATOM 2728 N LEU B 154 28.824 42.249 13.808 1.00 27.28 B N ATOM 2729 CA LEU B 154 29.898 41.662 14.576 1.00 27.94 B C ATOM 2730 CB LEU B 154 29.356 41.010 15.849 1.00 28.66 B C ATOM 2731 CG LEU B 154 28.459 41.877 16.723 1.00 25.37 B C ATOM 2732 CD1 LEU B 154 27.870 41.007 17.805 1.00 26.39 B C ATOM 2733 CD2 LEU B 154 29.255 43.029 17.309 1.00 27.92 B C ATOM 2734 C LEU B 154 30.671 40.626 13.791 1.00 27.39 B C ATOM 2735 O LEU B 154 30.124 39.973 12.903 1.00 27.85 B O ATOM 2736 N THR B 155 31.940 40.466 14.145 1.00 24.79 B N ATOM 2737 CA THR B 155 32.719 39.338 13.662 1.00 29.99 B C ATOM 2738 CB THR B 155 33.955 39.749 12.835 1.00 29.11 B C ATOM 2739 OG1 THR B 155 34.854 40.480 13.668 1.00 35.35 B O ATOM 2740 CG2 THR B 155 33.559 40.599 11.637 1.00 27.55 B C ATOM 2741 C THR B 155 33.198 38.549 14.860 1.00 29.95 B C ATOM 2742 O THR B 155 33.312 39.074 15.975 1.00 30.51 B O ATOM 2743 N PHE B 156 33.477 37.281 14.629 1.00 24.60 B N ATOM 2744 CA PHE B 156 33.935 36.423 15.704 1.00 26.60 B C ATOM 2745 CB PHE B 156 32.865 35.373 16.003 1.00 23.69 B C ATOM 2746 CG PHE B 156 31.556 35.994 16.453 1.00 23.37 B C ATOM 2747 CD1 PHE B 156 30.553 36.268 15.535 1.00 23.79 B C ATOM 2748 CD2 PHE B 156 31.372 36.379 17.774 1.00 23.42 B C ATOM 2749 CE1 PHE B 156 29.370 36.860 15.927 1.00 25.80 B C ATOM 2750 CE2 PHE B 156 30.180 36.984 18.188 1.00 25.22 B C ATOM 2751 CZ PHE B 156 29.182 37.228 17.273 1.00 25.13 B C ATOM 2752 C PHE B 156 35.293 35.822 15.365 1.00 31.67 B C ATOM 2753 O PHE B 156 35.500 35.315 14.264 1.00 27.33 B O ATOM 2754 N THR B 157 36.219 35.925 16.313 1.00 28.54 B N ATOM 2755 CA THR B 157 37.558 35.407 16.134 1.00 27.69 B C ATOM 2756 CB THR B 157 38.584 36.546 16.047 1.00 30.70 B C ATOM 2757 OG1 THR B 157 38.215 37.437 14.988 1.00 29.98 B O ATOM 2758 CG2 THR B 157 39.958 35.973 15.782 1.00 29.68 B C ATOM 2759 C THR B 157 37.989 34.495 17.263 1.00 25.50 B C ATOM 2760 O THR B 157 38.026 34.891 18.425 1.00 26.65 B O ATOM 2761 N ARG B 158 38.349 33.275 16.902 1.00 29.35 B N ATOM 2762 CA ARG B 158 38.915 32.324 17.835 1.00 29.60 B C ATOM 2763 CB ARG B 158 39.000 30.949 17.181 1.00 27.91 B C ATOM 2764 CG ARG B 158 39.496 29.883 18.130 1.00 34.73 B C ATOM 2765 CD ARG B 158 39.527 28.529 17.476 1.00 34.77 B C ATOM 2766 NE ARG B 158 40.155 27.541 18.346 1.00 37.19 B N ATOM 2767 CZ ARG B 158 40.381 26.285 17.981 1.00 39.32 B C ATOM 2768 NH1 ARG B 158 40.017 25.883 16.764 1.00 36.71 B N ATOM 2769 NH2 ARG B 158 40.957 25.431 18.823 1.00 38.34 B N ATOM 2770 C ARG B 158 40.315 32.755 18.261 1.00 32.28 B C ATOM 2771 O ARG B 158 41.173 33.025 17.415 1.00 29.12 B O ATOM 2772 N VAL B 159 40.535 32.810 19.568 1.00 28.37 B N ATOM 2773 CA VAL B 159 41.842 33.141 20.132 1.00 27.72 B C ATOM 2774 CB VAL B 159 41.823 34.529 20.753 1.00 28.76 B C ATOM 2775 CG1 VAL B 159 41.332 35.520 19.736 1.00 28.39 B C ATOM 2776 CG2 VAL B 159 40.915 34.536 21.969 1.00 30.12 B C ATOM 2777 C VAL B 159 42.216 32.118 21.206 1.00 32.99 B C ATOM 2778 O VAL B 159 41.384 31.314 21.621 1.00 31.96 B O ATOM 2779 N TYR B 160 43.461 32.148 21.667 1.00 32.91 B N ATOM 2780 CA TYR B 160 43.928 31.090 22.545 1.00 32.04 B C ATOM 2781 CB TYR B 160 44.975 30.222 21.839 1.00 35.20 B C ATOM 2782 CG TYR B 160 44.429 29.590 20.566 1.00 37.07 B C ATOM 2783 CD1 TYR B 160 44.273 30.344 19.412 1.00 31.16 B C ATOM 2784 CE1 TYR B 160 43.751 29.793 18.256 1.00 31.39 B C ATOM 2785 CD2 TYR B 160 44.039 28.249 20.530 1.00 34.44 B C ATOM 2786 CE2 TYR B 160 43.524 27.686 19.365 1.00 35.45 B C ATOM 2787 CZ TYR B 160 43.386 28.466 18.231 1.00 32.61 B C ATOM 2788 OH TYR B 160 42.882 27.945 17.057 1.00 36.36 B O ATOM 2789 C TYR B 160 44.431 31.622 23.875 1.00 35.22 B C ATOM 2790 O TYR B 160 45.254 30.985 24.535 1.00 45.29 B O ATOM 2791 N SER B 161 43.902 32.772 24.275 1.00 34.87 B N ATOM 2792 CA SER B 161 44.270 33.417 25.533 1.00 41.12 B C ATOM 2793 CB SER B 161 44.785 34.821 25.247 1.00 38.82 B C ATOM 2794 OG SER B 161 43.920 35.463 24.308 1.00 42.28 B O ATOM 2795 C SER B 161 43.061 33.547 26.459 1.00 40.99 B C ATOM 2796 O SER B 161 41.936 33.706 25.988 1.00 38.87 B O ATOM 2797 N ARG B 162 43.313 33.506 27.773 1.00 39.83 B N ATOM 2798 CA ARG B 162 42.322 33.843 28.807 1.00 43.33 B C ATOM 2799 CB ARG B 162 43.006 33.990 30.176 1.00 39.96 B C ATOM 2800 CG ARG B 162 44.114 32.973 30.432 1.00 45.70 B C ATOM 2801 CD ARG B 162 44.435 32.830 31.923 1.00 46.09 B C ATOM 2802 NE ARG B 162 44.847 31.467 32.254 1.00 42.10 B N ATOM 2803 CZ ARG B 162 46.093 31.006 32.152 1.00 48.05 B C ATOM 2804 NH1 ARG B 162 46.361 29.744 32.469 1.00 42.62 B N ATOM 2805 NH2 ARG B 162 47.073 31.796 31.722 1.00 52.85 B N ATOM 2806 C ARG B 162 41.680 35.168 28.447 1.00 38.45 B C ATOM 2807 O ARG B 162 40.586 35.487 28.870 1.00 40.31 B O ATOM 2808 N ASP B 163 42.408 35.934 27.652 1.00 42.88 B N ATOM 2809 CA ASP B 163 41.986 37.227 27.157 1.00 45.44 B C ATOM 2810 CB ASP B 163 43.235 37.960 26.659 1.00 50.05 B C ATOM 2811 CG ASP B 163 43.003 39.428 26.411 1.00 57.19 B C ATOM 2812 OD1 ASP B 163 41.911 39.931 26.753 1.00 57.70 B O ATOM 2813 OD2 ASP B 163 43.928 40.082 25.876 1.00 61.70 B O ATOM 2814 C ASP B 163 40.995 37.049 26.001 1.00 44.87 B C ATOM 2815 O ASP B 163 41.383 37.127 24.830 1.00 47.11 B O ATOM 2816 N ALA B 164 39.727 36.804 26.321 1.00 36.45 B N ATOM 2817 CA ALA B 164 38.688 36.707 25.289 1.00 35.94 B C ATOM 2818 CB ALA B 164 38.566 35.275 24.760 1.00 31.47 B C ATOM 2819 C ALA B 164 37.348 37.180 25.827 1.00 32.25 B C ATOM 2820 O ALA B 164 37.060 36.997 27.014 1.00 31.97 B O ATOM 2821 N ASP B 165 36.536 37.778 24.961 1.00 26.78 B N ATOM 2822 CA ASP B 165 35.185 38.212 25.330 1.00 28.79 B C ATOM 2823 CB ASP B 165 34.497 38.892 24.155 1.00 26.89 B C ATOM 2824 CG ASP B 165 35.208 40.140 23.718 1.00 30.96 B C ATOM 2825 OD1 ASP B 165 35.601 40.923 24.611 1.00 34.09 B O ATOM 2826 OD2 ASP B 165 35.362 40.341 22.497 1.00 30.82 B O ATOM 2827 C ASP B 165 34.325 37.042 25.777 1.00 29.43 B C ATOM 2828 O ASP B 165 33.646 37.109 26.791 1.00 31.68 B O ATOM 2829 N ILE B 166 34.355 35.973 24.996 1.00 29.02 B N ATOM 2830 CA ILE B 166 33.544 34.796 25.263 1.00 29.87 B C ATOM 2831 CB ILE B 166 32.663 34.454 24.058 1.00 28.39 B C ATOM 2832 CG2 ILE B 166 31.974 33.093 24.262 1.00 28.15 B C ATOM 2833 CG1 ILE B 166 31.653 35.578 23.812 1.00 27.02 B C ATOM 2834 CD1 ILE B 166 30.960 35.504 22.444 1.00 28.61 B C ATOM 2835 C ILE B 166 34.430 33.601 25.559 1.00 32.24 B C ATOM 2836 O ILE B 166 35.155 33.123 24.682 1.00 31.05 B O ATOM 2837 N VAL B 167 34.382 33.127 26.798 1.00 28.53 B N ATOM 2838 CA VAL B 167 35.070 31.902 27.137 1.00 27.88 B C ATOM 2839 CB VAL B 167 35.752 31.963 28.509 1.00 31.01 B C ATOM 2840 CG1 VAL B 167 36.429 30.631 28.812 1.00 30.45 B C ATOM 2841 CG2 VAL B 167 36.764 33.092 28.541 1.00 31.73 B C ATOM 2842 C VAL B 167 34.096 30.745 27.088 1.00 30.88 B C ATOM 2843 O VAL B 167 32.980 30.826 27.606 1.00 29.36 B O ATOM 2844 N ILE B 168 34.538 29.672 26.450 1.00 33.42 B N ATOM 2845 CA ILE B 168 33.734 28.485 26.215 1.00 31.33 B C ATOM 2846 CB ILE B 168 33.719 28.145 24.728 1.00 29.99 B C ATOM 2847 CG2 ILE B 168 33.089 26.781 24.494 1.00 32.16 B C ATOM 2848 CG1 ILE B 168 32.948 29.208 23.947 1.00 30.82 B C ATOM 2849 CD1 ILE B 168 33.193 29.134 22.443 1.00 28.53 B C ATOM 2850 C ILE B 168 34.316 27.303 26.980 1.00 31.59 B C ATOM 2851 O ILE B 168 35.510 27.000 26.865 1.00 29.89 B O ATOM 2852 N GLN B 169 33.458 26.631 27.736 1.00 29.41 B N ATOM 2853 CA GLN B 169 33.884 25.618 28.687 1.00 31.97 B C ATOM 2854 CB GLN B 169 33.955 26.236 30.092 1.00 32.01 B C ATOM 2855 CG GLN B 169 34.303 25.259 31.203 1.00 32.93 B C ATOM 2856 CD GLN B 169 33.967 25.804 32.593 1.00 38.34 B C ATOM 2857 OE1 GLN B 169 33.703 27.001 32.770 1.00 36.87 B O ATOM 2858 NE2 GLN B 169 33.970 24.921 33.586 1.00 41.49 B N ATOM 2859 C GLN B 169 32.915 24.439 28.711 1.00 32.73 B C ATOM 2860 O GLN B 169 31.687 24.612 28.685 1.00 30.74 B O ATOM 2861 N PHE B 170 33.471 23.239 28.758 1.00 26.71 B N ATOM 2862 CA PHE B 170 32.683 22.054 29.036 1.00 28.25 B C ATOM 2863 CB PHE B 170 33.167 20.870 28.213 1.00 30.26 B C ATOM 2864 CG PHE B 170 32.809 20.949 26.755 1.00 30.60 B C ATOM 2865 CD1 PHE B 170 33.677 21.527 25.845 1.00 30.32 B C ATOM 2866 CD2 PHE B 170 31.599 20.449 26.297 1.00 25.64 B C ATOM 2867 CE1 PHE B 170 33.348 21.595 24.492 1.00 29.60 B C ATOM 2868 CE2 PHE B 170 31.262 20.515 24.952 1.00 28.27 B C ATOM 2869 CZ PHE B 170 32.145 21.084 24.047 1.00 26.92 B C ATOM 2870 C PHE B 170 32.873 21.752 30.512 1.00 32.69 B C ATOM 2871 O PHE B 170 33.985 21.841 31.034 1.00 29.75 B O ATOM 2872 N GLY B 171 31.793 21.402 31.189 1.00 27.89 B N ATOM 2873 CA GLY B 171 31.866 21.155 32.622 1.00 34.82 B C ATOM 2874 C GLY B 171 30.762 20.228 33.079 1.00 31.42 B C ATOM 2875 O GLY B 171 29.810 19.990 32.344 1.00 33.00 B O ATOM 2876 N VAL B 172 30.894 19.689 34.283 1.00 32.50 B N ATOM 2877 CA VAL B 172 29.854 18.850 34.861 1.00 32.40 B C ATOM 2878 CB VAL B 172 30.270 17.362 34.879 1.00 36.95 B C ATOM 2879 CG1 VAL B 172 30.585 16.866 33.473 1.00 37.14 B C ATOM 2880 CG2 VAL B 172 31.474 17.166 35.768 1.00 36.23 B C ATOM 2881 C VAL B 172 29.578 19.318 36.288 1.00 38.27 B C ATOM 2882 O VAL B 172 30.458 19.889 36.951 1.00 37.37 B O ATOM 2883 N ALA B 173 28.355 19.091 36.754 1.00 35.47 B N ATOM 2884 CA ALA B 173 27.990 19.458 38.111 1.00 39.26 B C ATOM 2885 CB ALA B 173 28.642 18.499 39.099 1.00 44.27 B C ATOM 2886 C ALA B 173 28.405 20.893 38.423 1.00 39.51 B C ATOM 2887 O ALA B 173 28.210 21.804 37.626 1.00 34.77 B O ATOM 2888 N GLU B 174 28.972 21.101 39.602 1.00 42.22 B N ATOM 2889 CA GLU B 174 29.447 22.433 39.939 1.00 39.75 B C ATOM 2890 CB GLU B 174 29.559 22.624 41.451 1.00 40.66 B C ATOM 2891 CG GLU B 174 30.347 23.854 41.828 1.00 41.08 B C ATOM 2892 CD GLU B 174 29.686 25.146 41.383 1.00 43.32 B C ATOM 2893 OE1 GLU B 174 28.449 25.296 41.555 1.00 42.55 B O ATOM 2894 OE2 GLU B 174 30.420 26.024 40.872 1.00 49.18 B O ATOM 2895 C GLU B 174 30.788 22.613 39.265 1.00 41.68 B C ATOM 2896 O GLU B 174 31.723 21.851 39.502 1.00 44.37 B O ATOM 2897 N HIS B 175 30.882 23.617 38.408 1.00 39.73 B N ATOM 2898 CA HIS B 175 32.017 23.708 37.513 1.00 38.47 B C ATOM 2899 CB HIS B 175 31.579 23.330 36.109 1.00 35.46 B C ATOM 2900 CG HIS B 175 30.422 24.137 35.627 1.00 34.72 B C ATOM 2901 CD2 HIS B 175 30.364 25.274 34.895 1.00 28.68 B C ATOM 2902 ND1 HIS B 175 29.116 23.819 35.936 1.00 34.27 B N ATOM 2903 CE1 HIS B 175 28.305 24.715 35.402 1.00 32.11 B C ATOM 2904 NE2 HIS B 175 29.042 25.607 34.765 1.00 32.38 B N ATOM 2905 C HIS B 175 32.554 25.118 37.497 1.00 38.59 B C ATOM 2906 O HIS B 175 33.083 25.565 36.479 1.00 35.90 B O ATOM 2907 N GLY B 176 32.382 25.829 38.611 1.00 39.98 B N ATOM 2908 CA GLY B 176 33.099 27.074 38.824 1.00 39.34 B C ATOM 2909 C GLY B 176 32.338 28.386 38.747 1.00 39.39 B C ATOM 2910 O GLY B 176 32.966 29.447 38.761 1.00 44.45 B O ATOM 2911 N ASP B 177 31.010 28.344 38.665 1.00 40.58 B N ATOM 2912 CA ASP B 177 30.244 29.593 38.590 1.00 37.71 B C ATOM 2913 CB ASP B 177 29.842 29.936 37.153 1.00 35.17 B C ATOM 2914 CG ASP B 177 28.959 28.876 36.508 1.00 35.44 B C ATOM 2915 OD1 ASP B 177 28.653 29.054 35.309 1.00 37.17 B O ATOM 2916 OD2 ASP B 177 28.580 27.883 37.165 1.00 32.28 B O ATOM 2917 C ASP B 177 29.027 29.634 39.484 1.00 37.13 B C ATOM 2918 O ASP B 177 28.307 30.631 39.515 1.00 40.45 B O ATOM 2919 N GLY B 178 28.780 28.553 40.208 1.00 39.36 B N ATOM 2920 CA GLY B 178 27.684 28.547 41.166 1.00 41.81 B C ATOM 2921 C GLY B 178 26.330 28.247 40.559 1.00 42.36 B C ATOM 2922 O GLY B 178 25.317 28.264 41.255 1.00 39.75 B O ATOM 2923 N TYR B 179 26.305 27.971 39.257 1.00 40.36 B N ATOM 2924 CA TYR B 179 25.076 27.534 38.608 1.00 35.46 B C ATOM 2925 CB TYR B 179 24.731 28.441 37.443 1.00 36.29 B C ATOM 2926 CG TYR B 179 24.408 29.847 37.863 1.00 38.04 B C ATOM 2927 CD1 TYR B 179 25.372 30.836 37.829 1.00 37.78 B C ATOM 2928 CE1 TYR B 179 25.082 32.127 38.214 1.00 41.09 B C ATOM 2929 CD2 TYR B 179 23.133 30.187 38.304 1.00 42.02 B C ATOM 2930 CE2 TYR B 179 22.835 31.482 38.695 1.00 42.04 B C ATOM 2931 CZ TYR B 179 23.818 32.448 38.642 1.00 39.14 B C ATOM 2932 OH TYR B 179 23.546 33.743 39.015 1.00 40.80 B O ATOM 2933 C TYR B 179 25.286 26.115 38.135 1.00 37.63 B C ATOM 2934 O TYR B 179 25.366 25.852 36.937 1.00 36.12 B O ATOM 2935 N PRO B 180 25.386 25.186 39.086 1.00 36.78 B N ATOM 2936 CD PRO B 180 24.780 25.319 40.422 1.00 37.76 B C ATOM 2937 CA PRO B 180 25.804 23.816 38.765 1.00 37.27 B C ATOM 2938 CB PRO B 180 25.582 23.044 40.078 1.00 36.28 B C ATOM 2939 CG PRO B 180 25.089 24.019 41.088 1.00 36.47 B C ATOM 2940 C PRO B 180 24.935 23.184 37.690 1.00 35.05 B C ATOM 2941 O PRO B 180 23.726 23.441 37.661 1.00 35.80 B O ATOM 2942 N PHE B 181 25.531 22.356 36.834 1.00 31.34 B N ATOM 2943 CA PHE B 181 24.750 21.494 35.952 1.00 33.39 B C ATOM 2944 C PHE B 181 24.185 20.320 36.756 1.00 39.31 B C ATOM 2945 CB PHE B 181 25.596 20.993 34.779 1.00 35.46 B C ATOM 2946 CG PHE B 181 25.874 22.054 33.741 1.00 33.22 B C ATOM 2947 CD1 PHE B 181 24.874 22.924 33.339 1.00 30.55 B C ATOM 2948 CD2 PHE B 181 27.130 22.176 33.170 1.00 31.64 B C ATOM 2949 CE1 PHE B 181 25.120 23.910 32.390 1.00 29.68 B C ATOM 2950 CE2 PHE B 181 27.387 23.162 32.223 1.00 32.74 B C ATOM 2951 CZ PHE B 181 26.380 24.027 31.835 1.00 28.01 B C ATOM 2952 O PHE B 181 24.538 20.140 37.929 1.00 38.42 B O ATOM 2953 N ASP B 182 23.342 19.512 36.115 1.00 35.36 B N ATOM 2954 CA ASP B 182 22.515 18.528 36.814 1.00 40.36 B C ATOM 2955 CB ASP B 182 21.027 18.898 36.670 1.00 40.75 B C ATOM 2956 CG ASP B 182 20.598 19.042 35.203 1.00 39.50 B C ATOM 2957 OD1 ASP B 182 21.490 19.130 34.344 1.00 38.34 B O ATOM 2958 OD2 ASP B 182 19.382 19.069 34.910 1.00 36.39 B O ATOM 2959 C ASP B 182 22.696 17.097 36.315 1.00 40.67 B C ATOM 2960 O ASP B 182 21.728 16.343 36.243 1.00 44.49 B O ATOM 2961 N GLY B 183 23.911 16.707 35.964 1.00 39.11 B N ATOM 2962 CA GLY B 183 24.082 15.379 35.404 1.00 39.73 B C ATOM 2963 C GLY B 183 23.279 15.266 34.117 1.00 41.17 B C ATOM 2964 O GLY B 183 22.825 16.270 33.588 1.00 38.13 B O ATOM 2965 N LYS B 184 23.078 14.048 33.626 1.00 42.72 B N ATOM 2966 CA LYS B 184 22.506 13.844 32.294 1.00 42.30 B C ATOM 2967 CB LYS B 184 22.756 12.402 31.826 1.00 41.63 B C ATOM 2968 CG LYS B 184 21.534 11.513 31.664 1.00 41.85 B C ATOM 2969 CD LYS B 184 21.970 10.175 31.071 1.00 48.21 B C ATOM 2970 CE LYS B 184 20.803 9.297 30.632 1.00 53.57 B C ATOM 2971 NZ LYS B 184 21.302 7.981 30.099 1.00 55.55 B N ATOM 2972 C LYS B 184 21.039 14.286 32.117 1.00 42.70 B C ATOM 2973 O LYS B 184 20.227 14.166 33.033 1.00 43.78 B O ATOM 2974 N ASP B 185 20.728 14.809 30.929 1.00 41.43 B N ATOM 2975 CA ASP B 185 19.416 15.381 30.616 1.00 42.41 B C ATOM 2976 CB ASP B 185 18.311 14.348 30.780 1.00 41.58 B C ATOM 2977 CG ASP B 185 18.282 13.367 29.636 1.00 45.03 B C ATOM 2978 OD1 ASP B 185 19.179 13.445 28.763 1.00 48.74 B O ATOM 2979 OD2 ASP B 185 17.369 12.519 29.608 1.00 51.18 B O ATOM 2980 C ASP B 185 19.109 16.637 31.419 1.00 39.33 B C ATOM 2981 O ASP B 185 19.977 17.176 32.066 1.00 42.69 B O ATOM 2982 N GLY B 186 17.877 17.118 31.372 1.00 39.95 B N ATOM 2983 CA GLY B 186 17.560 18.371 32.042 1.00 38.62 B C ATOM 2984 C GLY B 186 18.232 19.576 31.383 1.00 39.16 B C ATOM 2985 O GLY B 186 18.030 19.823 30.188 1.00 36.26 B O ATOM 2986 N LEU B 187 19.000 20.336 32.168 1.00 35.71 B N ATOM 2987 CA LEU B 187 19.750 21.486 31.660 1.00 36.50 B C ATOM 2988 CB LEU B 187 20.459 22.226 32.796 1.00 38.70 B C ATOM 2989 CG LEU B 187 19.679 22.963 33.874 1.00 39.93 B C ATOM 2990 CD1 LEU B 187 18.897 21.982 34.675 1.00 37.98 B C ATOM 2991 CD2 LEU B 187 20.653 23.721 34.761 1.00 41.27 B C ATOM 2992 C LEU B 187 20.830 21.000 30.722 1.00 36.17 B C ATOM 2993 O LEU B 187 21.590 20.129 31.095 1.00 33.95 B O ATOM 2994 N LEU B 188 20.941 21.589 29.536 1.00 31.56 B N ATOM 2995 CA LEU B 188 21.957 21.147 28.584 1.00 30.02 B C ATOM 2996 CB LEU B 188 21.368 21.099 27.175 1.00 33.46 B C ATOM 2997 CG LEU B 188 20.261 20.051 27.020 1.00 33.86 B C ATOM 2998 CD1 LEU B 188 19.708 20.032 25.599 1.00 27.68 B C ATOM 2999 CD2 LEU B 188 20.791 18.670 27.437 1.00 32.75 B C ATOM 3000 C LEU B 188 23.206 22.028 28.593 1.00 30.77 B C ATOM 3001 O LEU B 188 24.313 21.559 28.296 1.00 30.19 B O ATOM 3002 N ALA B 189 23.016 23.297 28.942 1.00 26.98 B N ATOM 3003 CA ALA B 189 24.068 24.288 28.844 1.00 29.14 B C ATOM 3004 CB ALA B 189 24.494 24.443 27.368 1.00 25.83 B C ATOM 3005 C ALA B 189 23.495 25.596 29.351 1.00 28.17 B C ATOM 3006 O ALA B 189 22.294 25.699 29.571 1.00 25.95 B O ATOM 3007 N HIS B 190 24.342 26.608 29.509 1.00 26.71 B N ATOM 3008 CA HIS B 190 23.846 27.942 29.818 1.00 26.54 B C ATOM 3009 CB HIS B 190 23.406 28.039 31.296 1.00 25.95 B C ATOM 3010 CG HIS B 190 24.508 27.769 32.280 1.00 28.88 B C ATOM 3011 CD2 HIS B 190 25.842 27.979 32.194 1.00 29.68 B C ATOM 3012 ND1 HIS B 190 24.285 27.236 33.534 1.00 29.27 B N ATOM 3013 CE1 HIS B 190 25.434 27.118 34.171 1.00 26.95 B C ATOM 3014 NE2 HIS B 190 26.394 27.562 33.385 1.00 32.38 B N ATOM 3015 C HIS B 190 24.904 28.970 29.469 1.00 23.85 B C ATOM 3016 O HIS B 190 26.034 28.615 29.188 1.00 29.09 B O ATOM 3017 N ALA B 191 24.545 30.244 29.474 1.00 27.11 B N ATOM 3018 CA ALA B 191 25.490 31.283 29.081 1.00 27.02 B C ATOM 3019 CB ALA B 191 25.479 31.463 27.556 1.00 25.05 B C ATOM 3020 C ALA B 191 25.149 32.598 29.781 1.00 30.46 B C ATOM 3021 O ALA B 191 24.083 32.729 30.370 1.00 29.13 B O ATOM 3022 N PHE B 192 26.050 33.570 29.689 1.00 28.27 B N ATOM 3023 CA PHE B 192 25.913 34.835 30.395 1.00 30.24 B C ATOM 3024 CB PHE B 192 27.062 34.975 31.387 1.00 30.73 B C ATOM 3025 CG PHE B 192 27.161 33.818 32.331 1.00 35.41 B C ATOM 3026 CD1 PHE B 192 26.489 33.837 33.553 1.00 37.09 B C ATOM 3027 CD2 PHE B 192 27.870 32.685 31.984 1.00 31.08 B C ATOM 3028 CE1 PHE B 192 26.557 32.742 34.419 1.00 37.81 B C ATOM 3029 CE2 PHE B 192 27.935 31.587 32.844 1.00 32.68 B C ATOM 3030 CZ PHE B 192 27.295 31.617 34.055 1.00 33.09 B C ATOM 3031 C PHE B 192 25.899 35.992 29.401 1.00 32.03 B C ATOM 3032 O PHE B 192 26.529 35.904 28.355 1.00 29.16 B O ATOM 3033 N PRO B 193 25.156 37.067 29.708 1.00 30.58 B N ATOM 3034 CD PRO B 193 24.405 37.324 30.946 1.00 32.89 B C ATOM 3035 CA PRO B 193 25.027 38.166 28.743 1.00 29.36 B C ATOM 3036 CB PRO B 193 23.961 39.068 29.382 1.00 30.69 B C ATOM 3037 CG PRO B 193 24.074 38.784 30.836 1.00 36.85 B C ATOM 3038 C PRO B 193 26.340 38.918 28.580 1.00 30.03 B C ATOM 3039 O PRO B 193 27.234 38.781 29.406 1.00 33.29 B O ATOM 3040 N PRO B 194 26.464 39.708 27.512 1.00 30.53 B N ATOM 3041 CD PRO B 194 25.441 39.966 26.488 1.00 30.19 B C ATOM 3042 CA PRO B 194 27.711 40.424 27.241 1.00 28.06 B C ATOM 3043 CB PRO B 194 27.341 41.321 26.053 1.00 29.96 B C ATOM 3044 CG PRO B 194 26.230 40.597 25.370 1.00 26.21 B C ATOM 3045 C PRO B 194 28.139 41.277 28.426 1.00 31.83 B C ATOM 3046 O PRO B 194 27.302 41.781 29.180 1.00 30.07 B O ATOM 3047 N GLY B 195 29.446 41.437 28.588 1.00 34.84 B N ATOM 3048 CA GLY B 195 29.979 42.215 29.690 1.00 36.64 B C ATOM 3049 C GLY B 195 31.275 41.626 30.201 1.00 34.71 B C ATOM 3050 O GLY B 195 31.883 40.804 29.521 1.00 36.67 B O ATOM 3051 N PRO B 196 31.690 42.031 31.410 1.00 34.14 B N ATOM 3052 CD PRO B 196 30.951 42.975 32.258 1.00 40.61 B C ATOM 3053 CA PRO B 196 33.012 41.727 31.964 1.00 39.50 B C ATOM 3054 CB PRO B 196 33.202 42.801 33.047 1.00 40.08 B C ATOM 3055 CG PRO B 196 32.053 43.760 32.887 1.00 43.18 B C ATOM 3056 C PRO B 196 33.095 40.350 32.601 1.00 37.52 B C ATOM 3057 O PRO B 196 32.083 39.772 32.960 1.00 36.46 B O ATOM 3058 N GLY B 197 34.314 39.836 32.720 1.00 44.77 B N ATOM 3059 CA GLY B 197 34.567 38.593 33.425 1.00 42.13 B C ATOM 3060 C GLY B 197 33.804 37.404 32.886 1.00 38.29 B C ATOM 3061 O GLY B 197 34.083 36.921 31.801 1.00 40.29 B O ATOM 3062 N ILE B 198 32.843 36.921 33.656 1.00 38.79 B N ATOM 3063 CA ILE B 198 32.120 35.714 33.288 1.00 39.25 B C ATOM 3064 CB ILE B 198 31.498 35.051 34.522 1.00 39.24 B C ATOM 3065 CG2 ILE B 198 30.209 35.775 34.951 1.00 39.98 B C ATOM 3066 CG1 ILE B 198 31.254 33.566 34.257 1.00 38.75 B C ATOM 3067 CD1 ILE B 198 30.582 32.855 35.417 1.00 37.74 B C ATOM 3068 C ILE B 198 31.048 36.020 32.241 1.00 37.80 B C ATOM 3069 O ILE B 198 30.555 35.126 31.550 1.00 35.85 B O ATOM 3070 N GLN B 199 30.715 37.297 32.120 1.00 35.98 B N ATOM 3071 CA GLN B 199 29.706 37.732 31.178 1.00 34.37 B C ATOM 3072 CB GLN B 199 29.303 39.182 31.454 1.00 34.35 B C ATOM 3073 CG GLN B 199 28.569 39.310 32.787 1.00 36.08 B C ATOM 3074 CD GLN B 199 28.184 40.741 33.139 1.00 42.98 B C ATOM 3075 OE1 GLN B 199 28.174 41.113 34.318 1.00 36.41 B O ATOM 3076 NE2 GLN B 199 27.862 41.549 32.120 1.00 36.93 B N ATOM 3077 C GLN B 199 30.177 37.526 29.754 1.00 30.87 B C ATOM 3078 O GLN B 199 31.272 37.936 29.395 1.00 33.70 B O ATOM 3079 N GLY B 200 29.329 36.889 28.956 1.00 30.36 B N ATOM 3080 CA GLY B 200 29.661 36.497 27.599 1.00 28.96 B C ATOM 3081 C GLY B 200 30.033 35.028 27.460 1.00 27.79 B C ATOM 3082 O GLY B 200 29.979 34.472 26.376 1.00 30.58 B O ATOM 3083 N ASP B 201 30.426 34.400 28.559 1.00 31.76 B N ATOM 3084 CA ASP B 201 30.848 33.002 28.544 1.00 30.84 B C ATOM 3085 CB ASP B 201 31.503 32.636 29.879 1.00 30.86 B C ATOM 3086 CG ASP B 201 32.795 33.364 30.093 1.00 35.26 B C ATOM 3087 OD1 ASP B 201 33.144 34.167 29.205 1.00 34.12 B O ATOM 3088 OD2 ASP B 201 33.468 33.125 31.118 1.00 39.43 B O ATOM 3089 C ASP B 201 29.702 32.038 28.293 1.00 31.82 B C ATOM 3090 O ASP B 201 28.540 32.327 28.609 1.00 32.85 B O ATOM 3091 N ALA B 202 30.051 30.865 27.776 1.00 29.49 B N ATOM 3092 CA ALA B 202 29.078 29.833 27.454 1.00 28.11 B C ATOM 3093 CB ALA B 202 28.860 29.773 25.917 1.00 26.32 B C ATOM 3094 C ALA B 202 29.623 28.516 27.969 1.00 29.83 B C ATOM 3095 O ALA B 202 30.775 28.171 27.702 1.00 32.20 B O ATOM 3096 N HIS B 203 28.801 27.785 28.712 1.00 27.70 B N ATOM 3097 CA HIS B 203 29.207 26.518 29.307 1.00 28.19 B C ATOM 3098 CB HIS B 203 29.130 26.632 30.834 1.00 31.66 B C ATOM 3099 CG HIS B 203 29.961 27.743 31.398 1.00 33.16 B C ATOM 3100 CD2 HIS B 203 30.914 28.518 30.829 1.00 28.58 B C ATOM 3101 ND1 HIS B 203 29.854 28.159 32.711 1.00 32.21 B N ATOM 3102 CE1 HIS B 203 30.710 29.146 32.923 1.00 35.07 B C ATOM 3103 NE2 HIS B 203 31.369 29.374 31.807 1.00 36.96 B N ATOM 3104 C HIS B 203 28.291 25.390 28.831 1.00 28.56 B C ATOM 3105 O HIS B 203 27.097 25.594 28.644 1.00 29.79 B O ATOM 3106 N PHE B 204 28.849 24.200 28.661 1.00 28.04 B N ATOM 3107 CA PHE B 204 28.108 23.060 28.147 1.00 28.14 B C ATOM 3108 CB PHE B 204 28.627 22.670 26.745 1.00 29.02 B C ATOM 3109 CG PHE B 204 28.512 23.787 25.731 1.00 30.78 B C ATOM 3110 CD1 PHE B 204 29.478 24.776 25.657 1.00 28.76 B C ATOM 3111 CD2 PHE B 204 27.416 23.874 24.887 1.00 28.07 B C ATOM 3112 CE1 PHE B 204 29.360 25.818 24.755 1.00 24.40 B C ATOM 3113 CE2 PHE B 204 27.296 24.917 23.985 1.00 22.92 B C ATOM 3114 CZ PHE B 204 28.260 25.890 23.926 1.00 25.26 B C ATOM 3115 C PHE B 204 28.238 21.902 29.132 1.00 31.14 B C ATOM 3116 O PHE B 204 29.319 21.627 29.650 1.00 29.11 B O ATOM 3117 N ASP B 205 27.129 21.231 29.399 1.00 29.08 B N ATOM 3118 CA ASP B 205 27.124 20.161 30.376 1.00 30.87 B C ATOM 3119 CB ASP B 205 25.705 19.933 30.880 1.00 31.10 B C ATOM 3120 CG ASP B 205 25.637 18.921 32.010 1.00 34.12 B C ATOM 3121 OD1 ASP B 205 26.656 18.283 32.354 1.00 36.27 B O ATOM 3122 OD2 ASP B 205 24.540 18.762 32.559 1.00 34.71 B O ATOM 3123 C ASP B 205 27.682 18.887 29.782 1.00 30.35 B C ATOM 3124 O ASP B 205 27.051 18.251 28.945 1.00 32.08 B O ATOM 3125 N ASP B 206 28.862 18.496 30.229 1.00 32.42 B N ATOM 3126 CA ASP B 206 29.558 17.393 29.588 1.00 31.21 B C ATOM 3127 CB ASP B 206 31.065 17.545 29.755 1.00 32.15 B C ATOM 3128 CG ASP B 206 31.858 16.886 28.627 1.00 33.18 B C ATOM 3129 OD1 ASP B 206 31.242 16.355 27.669 1.00 32.03 B O ATOM 3130 OD2 ASP B 206 33.109 16.918 28.704 1.00 35.29 B O ATOM 3131 C ASP B 206 29.078 16.045 30.109 1.00 34.11 B C ATOM 3132 O ASP B 206 29.625 14.996 29.758 1.00 32.87 B O ATOM 3133 N ASP B 207 28.060 16.085 30.962 1.00 35.08 B N ATOM 3134 CA ASP B 207 27.328 14.882 31.335 1.00 37.04 B C ATOM 3135 CB ASP B 207 26.629 15.057 32.684 1.00 37.43 B C ATOM 3136 CG ASP B 207 27.485 14.599 33.837 1.00 38.06 B C ATOM 3137 OD1 ASP B 207 28.325 13.686 33.628 1.00 36.41 B O ATOM 3138 OD2 ASP B 207 27.319 15.161 34.941 1.00 34.60 B O ATOM 3139 C ASP B 207 26.306 14.540 30.261 1.00 35.39 B C ATOM 3140 O ASP B 207 25.656 13.508 30.327 1.00 33.03 B O ATOM 3141 N GLU B 208 26.154 15.427 29.283 1.00 34.95 B N ATOM 3142 CA GLU B 208 25.394 15.091 28.084 1.00 33.46 B C ATOM 3143 CB GLU B 208 24.770 16.336 27.450 1.00 33.55 B C ATOM 3144 CG GLU B 208 24.120 17.248 28.408 1.00 34.83 B C ATOM 3145 CD GLU B 208 22.953 16.598 29.113 1.00 38.78 B C ATOM 3146 OE1 GLU B 208 22.615 15.423 28.823 1.00 37.38 B O ATOM 3147 OE2 GLU B 208 22.363 17.288 29.949 1.00 38.50 B O ATOM 3148 C GLU B 208 26.317 14.474 27.054 1.00 32.20 B C ATOM 3149 O GLU B 208 27.492 14.823 26.973 1.00 33.36 B O ATOM 3150 N LEU B 209 25.769 13.574 26.251 1.00 32.49 B N ATOM 3151 CA LEU B 209 26.462 13.086 25.077 1.00 37.30 B C ATOM 3152 CB LEU B 209 25.850 11.774 24.606 1.00 38.67 B C ATOM 3153 CG LEU B 209 26.411 11.176 23.322 1.00 41.31 B C ATOM 3154 CD1 LEU B 209 27.776 10.551 23.573 1.00 36.31 B C ATOM 3155 CD2 LEU B 209 25.430 10.145 22.776 1.00 44.11 B C ATOM 3156 C LEU B 209 26.337 14.141 23.985 1.00 36.94 B C ATOM 3157 O LEU B 209 25.226 14.478 23.545 1.00 35.07 B O ATOM 3158 N TRP B 210 27.484 14.667 23.572 1.00 34.18 B N ATOM 3159 CA TRP B 210 27.541 15.716 22.568 1.00 34.84 B C ATOM 3160 CB TRP B 210 28.582 16.776 22.967 1.00 31.76 B C ATOM 3161 CG TRP B 210 28.096 17.586 24.115 1.00 29.94 B C ATOM 3162 CD2 TRP B 210 26.982 18.486 24.106 1.00 28.55 B C ATOM 3163 CE2 TRP B 210 26.849 18.997 25.412 1.00 31.19 B C ATOM 3164 CE3 TRP B 210 26.084 18.909 23.117 1.00 28.31 B C ATOM 3165 CD1 TRP B 210 28.572 17.575 25.397 1.00 28.82 B C ATOM 3166 NE1 TRP B 210 27.838 18.426 26.178 1.00 26.55 B N ATOM 3167 CZ2 TRP B 210 25.860 19.920 25.756 1.00 28.51 B C ATOM 3168 CZ3 TRP B 210 25.107 19.825 23.453 1.00 26.86 B C ATOM 3169 CH2 TRP B 210 24.998 20.318 24.767 1.00 28.13 B C ATOM 3170 C TRP B 210 27.853 15.126 21.206 1.00 31.28 B C ATOM 3171 O TRP B 210 28.832 14.405 21.043 1.00 28.86 B O ATOM 3172 N SER B 211 26.987 15.405 20.244 1.00 28.84 B N ATOM 3173 CA SER B 211 27.204 14.955 18.874 1.00 35.53 B C ATOM 3174 CB SER B 211 26.470 13.642 18.592 1.00 34.48 B C ATOM 3175 OG SER B 211 25.077 13.771 18.818 1.00 36.46 B O ATOM 3176 C SER B 211 26.719 16.031 17.918 1.00 33.41 B C ATOM 3177 O SER B 211 26.546 17.188 18.310 1.00 29.51 B O ATOM 3178 N LEU B 212 26.482 15.651 16.671 1.00 31.49 B N ATOM 3179 CA LEU B 212 25.926 16.612 15.747 1.00 34.36 B C ATOM 3180 CB LEU B 212 26.575 16.530 14.372 1.00 37.26 B C ATOM 3181 CG LEU B 212 28.009 17.022 14.531 1.00 35.51 B C ATOM 3182 CD1 LEU B 212 28.600 17.446 13.193 1.00 39.28 B C ATOM 3183 CD2 LEU B 212 28.016 18.191 15.496 1.00 32.06 B C ATOM 3184 C LEU B 212 24.426 16.495 15.715 1.00 38.47 B C ATOM 3185 O LEU B 212 23.780 16.959 14.769 1.00 42.85 B O ATOM 3186 N GLY B 213 23.902 15.898 16.794 1.00 38.85 B N ATOM 3187 CA GLY B 213 22.479 15.725 17.036 1.00 37.81 B C ATOM 3188 C GLY B 213 21.926 15.085 15.792 1.00 47.47 B C ATOM 3189 O GLY B 213 22.020 15.643 14.707 1.00 52.52 B O ATOM 3190 N LYS B 389 21.387 13.889 15.901 1.00 49.94 B N ATOM 3191 CA LYS B 389 21.121 13.140 14.677 1.00 52.59 B C ATOM 3192 CB LYS B 389 22.429 12.954 13.907 1.00 56.45 B C ATOM 3193 CG LYS B 389 22.389 13.449 12.480 1.00 55.44 B C ATOM 3194 CD LYS B 389 21.878 12.368 11.574 1.00 60.22 B C ATOM 3195 CE LYS B 389 22.573 12.447 10.225 1.00 63.58 B C ATOM 3196 NZ LYS B 389 22.625 11.084 9.603 1.00 66.66 B N ATOM 3197 C LYS B 389 20.481 11.787 14.970 1.00 50.63 B C ATOM 3198 O LYS B 389 19.587 11.340 14.260 1.00 52.27 B O ATOM 3199 N GLY B 390 20.943 11.154 16.041 1.00 50.77 B N ATOM 3200 CA GLY B 390 20.368 9.918 16.531 1.00 47.84 B C ATOM 3201 C GLY B 390 20.434 10.091 18.024 1.00 45.87 B C ATOM 3202 O GLY B 390 19.566 10.722 18.621 1.00 48.47 B O ATOM 3203 N GLN B 391 21.488 9.563 18.623 1.00 47.37 B N ATOM 3204 CA GLN B 391 21.785 9.856 20.013 1.00 52.04 B C ATOM 3205 CB GLN B 391 22.799 8.840 20.564 1.00 52.03 B C ATOM 3206 CG GLN B 391 24.135 8.775 19.769 1.00 50.55 B C ATOM 3207 CD GLN B 391 25.103 7.711 20.291 1.00 49.48 B C ATOM 3208 OE1 GLN B 391 24.694 6.740 20.930 1.00 58.51 B O ATOM 3209 NE2 GLN B 391 26.394 7.893 20.017 1.00 52.67 B N ATOM 3210 C GLN B 391 22.378 11.261 20.015 1.00 48.44 B C ATOM 3211 O GLN B 391 22.596 11.854 18.957 1.00 52.11 B O ATOM 3212 N GLY B 392 22.639 11.800 21.194 1.00 46.69 B N ATOM 3213 CA GLY B 392 23.388 13.034 21.280 1.00 39.31 B C ATOM 3214 C GLY B 392 22.590 14.300 21.032 1.00 37.93 B C ATOM 3215 O GLY B 392 21.698 14.365 20.183 1.00 36.55 B O ATOM 3216 N TYR B 393 22.923 15.315 21.815 1.00 36.88 B N ATOM 3217 CA TYR B 393 22.419 16.652 21.598 1.00 33.09 B C ATOM 3218 CB TYR B 393 22.347 17.404 22.933 1.00 27.70 B C ATOM 3219 CG TYR B 393 21.340 16.780 23.887 1.00 32.72 B C ATOM 3220 CD1 TYR B 393 19.980 17.039 23.751 1.00 30.68 B C ATOM 3221 CE1 TYR B 393 19.048 16.468 24.605 1.00 34.50 B C ATOM 3222 CD2 TYR B 393 21.746 15.923 24.905 1.00 29.49 B C ATOM 3223 CE2 TYR B 393 20.818 15.337 25.758 1.00 36.98 B C ATOM 3224 CZ TYR B 393 19.470 15.615 25.605 1.00 35.78 B C ATOM 3225 OH TYR B 393 18.542 15.052 26.456 1.00 38.17 B O ATOM 3226 C TYR B 393 23.399 17.323 20.645 1.00 28.88 B C ATOM 3227 O TYR B 393 24.604 17.169 20.788 1.00 28.18 B O ATOM 3228 N SER B 394 22.879 18.040 19.662 1.00 28.09 B N ATOM 3229 CA SER B 394 23.734 18.691 18.678 1.00 29.57 B C ATOM 3230 CB SER B 394 22.907 19.206 17.507 1.00 26.45 B C ATOM 3231 OG SER B 394 23.600 20.276 16.887 1.00 29.83 B O ATOM 3232 C SER B 394 24.473 19.862 19.319 1.00 28.00 B C ATOM 3233 O SER B 394 23.858 20.875 19.702 1.00 22.92 B O ATOM 3234 N LEU B 395 25.787 19.730 19.438 1.00 22.52 B N ATOM 3235 CA LEU B 395 26.575 20.812 20.013 1.00 24.75 B C ATOM 3236 CB LEU B 395 28.044 20.400 20.135 1.00 25.19 B C ATOM 3237 CG LEU B 395 29.044 21.415 20.681 1.00 27.43 B C ATOM 3238 CD1 LEU B 395 28.716 21.782 22.104 1.00 24.39 B C ATOM 3239 CD2 LEU B 395 30.477 20.863 20.581 1.00 22.97 B C ATOM 3240 C LEU B 395 26.423 22.043 19.134 1.00 23.50 B C ATOM 3241 O LEU B 395 26.467 23.173 19.609 1.00 23.15 B O ATOM 3242 N PHE B 396 26.238 21.828 17.836 1.00 23.81 B N ATOM 3243 CA PHE B 396 26.094 22.962 16.920 1.00 22.27 B C ATOM 3244 CB PHE B 396 25.959 22.497 15.461 1.00 21.83 B C ATOM 3245 CG PHE B 396 25.510 23.591 14.512 1.00 23.05 B C ATOM 3246 CD1 PHE B 396 26.271 24.756 14.353 1.00 23.29 B C ATOM 3247 CD2 PHE B 396 24.354 23.450 13.765 1.00 22.05 B C ATOM 3248 CE1 PHE B 396 25.868 25.763 13.467 1.00 23.00 B C ATOM 3249 CE2 PHE B 396 23.938 24.451 12.876 1.00 21.28 B C ATOM 3250 CZ PHE B 396 24.707 25.608 12.721 1.00 24.29 B C ATOM 3251 C PHE B 396 24.871 23.783 17.326 1.00 23.65 B C ATOM 3252 O PHE B 396 24.962 24.984 17.554 1.00 21.22 B O ATOM 3253 N LEU B 397 23.724 23.115 17.432 1.00 24.99 B N ATOM 3254 CA LEU B 397 22.476 23.813 17.692 1.00 26.82 B C ATOM 3255 CB LEU B 397 21.287 22.864 17.524 1.00 31.00 B C ATOM 3256 CG LEU B 397 21.005 22.351 16.104 1.00 26.82 B C ATOM 3257 CD1 LEU B 397 19.863 21.341 16.151 1.00 30.67 B C ATOM 3258 CD2 LEU B 397 20.663 23.508 15.147 1.00 23.55 B C ATOM 3259 C LEU B 397 22.471 24.461 19.081 1.00 26.40 B C ATOM 3260 O LEU B 397 22.021 25.589 19.239 1.00 24.64 B O ATOM 3261 N VAL B 398 22.973 23.745 20.081 1.00 24.73 B N ATOM 3262 CA VAL B 398 22.951 24.284 21.434 1.00 28.98 B C ATOM 3263 CB VAL B 398 23.287 23.228 22.512 1.00 29.57 B C ATOM 3264 CG1 VAL B 398 23.466 23.904 23.872 1.00 23.81 B C ATOM 3265 CG2 VAL B 398 22.202 22.158 22.573 1.00 28.14 B C ATOM 3266 C VAL B 398 23.928 25.451 21.519 1.00 26.33 B C ATOM 3267 O VAL B 398 23.656 26.443 22.195 1.00 26.03 B O ATOM 3268 N ALA B 399 25.071 25.321 20.848 1.00 24.27 B N ATOM 3269 CA ALA B 399 26.041 26.419 20.763 1.00 23.73 B C ATOM 3270 CB ALA B 399 27.277 25.994 19.977 1.00 25.97 B C ATOM 3271 C ALA B 399 25.436 27.673 20.141 1.00 25.18 B C ATOM 3272 O ALA B 399 25.627 28.782 20.652 1.00 25.18 B O ATOM 3273 N ALA B 400 24.715 27.507 19.035 1.00 23.76 B N ATOM 3274 CA ALA B 400 24.093 28.654 18.367 1.00 24.92 B C ATOM 3275 CB ALA B 400 23.365 28.219 17.123 1.00 23.60 B C ATOM 3276 C ALA B 400 23.133 29.336 19.324 1.00 24.65 B C ATOM 3277 O ALA B 400 23.055 30.562 19.394 1.00 25.21 B O ATOM 3278 N HIS B 401 22.403 28.525 20.068 1.00 23.72 B N ATOM 3279 CA HIS B 401 21.474 29.045 21.060 1.00 25.25 B C ATOM 3280 CB HIS B 401 20.700 27.917 21.726 1.00 24.20 B C ATOM 3281 CG HIS B 401 19.732 28.392 22.774 1.00 23.09 B C ATOM 3282 CD2 HIS B 401 19.911 28.670 24.095 1.00 23.50 B C ATOM 3283 ND1 HIS B 401 18.412 28.637 22.512 1.00 25.12 B N ATOM 3284 CE1 HIS B 401 17.799 29.050 23.610 1.00 24.70 B C ATOM 3285 NE2 HIS B 401 18.699 29.064 24.589 1.00 23.34 B N ATOM 3286 C HIS B 401 22.194 29.850 22.124 1.00 22.09 B C ATOM 3287 O HIS B 401 21.842 31.001 22.382 1.00 23.91 B O ATOM 3288 N GLU B 402 23.191 29.232 22.749 1.00 21.08 B N ATOM 3289 CA GLU B 402 23.896 29.855 23.863 1.00 23.01 B C ATOM 3290 CB GLU B 402 24.852 28.873 24.533 1.00 22.75 B C ATOM 3291 CG GLU B 402 24.175 27.633 25.065 1.00 23.67 B C ATOM 3292 CD GLU B 402 23.192 27.919 26.207 1.00 26.49 B C ATOM 3293 OE1 GLU B 402 23.290 28.999 26.849 1.00 21.30 B O ATOM 3294 OE2 GLU B 402 22.327 27.046 26.447 1.00 24.68 B O ATOM 3295 C GLU B 402 24.659 31.099 23.431 1.00 25.15 B C ATOM 3296 O GLU B 402 24.734 32.066 24.198 1.00 27.11 B O ATOM 3297 N PHE B 403 25.232 31.069 22.223 1.00 25.23 B N ATOM 3298 CA PHE B 403 25.943 32.226 21.674 1.00 22.98 B C ATOM 3299 CB PHE B 403 26.638 31.901 20.333 1.00 25.21 B C ATOM 3300 CG PHE B 403 27.778 30.900 20.436 1.00 23.91 B C ATOM 3301 CD1 PHE B 403 28.251 30.476 21.665 1.00 26.23 B C ATOM 3302 CD2 PHE B 403 28.376 30.390 19.286 1.00 26.21 B C ATOM 3303 CE1 PHE B 403 29.296 29.548 21.755 1.00 29.58 B C ATOM 3304 CE2 PHE B 403 29.429 29.478 19.363 1.00 25.67 B C ATOM 3305 CZ PHE B 403 29.886 29.051 20.602 1.00 23.72 B C ATOM 3306 C PHE B 403 24.945 33.388 21.506 1.00 24.86 B C ATOM 3307 O PHE B 403 25.314 34.555 21.567 1.00 22.93 B O ATOM 3308 N GLY B 404 23.678 33.052 21.284 1.00 24.77 B N ATOM 3309 CA GLY B 404 22.611 34.043 21.259 1.00 26.05 B C ATOM 3310 C GLY B 404 22.558 34.847 22.556 1.00 25.61 B C ATOM 3311 O GLY B 404 22.502 36.074 22.529 1.00 22.37 B O ATOM 3312 N HIS B 405 22.588 34.149 23.690 1.00 25.09 B N ATOM 3313 CA HIS B 405 22.668 34.801 25.010 1.00 27.23 B C ATOM 3314 CB HIS B 405 22.603 33.775 26.147 1.00 24.75 B C ATOM 3315 CG HIS B 405 21.289 33.070 26.287 1.00 26.55 B C ATOM 3316 CD2 HIS B 405 20.995 31.770 26.542 1.00 25.45 B C ATOM 3317 ND1 HIS B 405 20.078 33.727 26.223 1.00 27.85 B N ATOM 3318 CE1 HIS B 405 19.095 32.860 26.413 1.00 27.79 B C ATOM 3319 NE2 HIS B 405 19.632 31.668 26.606 1.00 24.97 B N ATOM 3320 C HIS B 405 23.968 35.604 25.167 1.00 27.09 B C ATOM 3321 O HIS B 405 23.951 36.710 25.699 1.00 23.77 B O ATOM 3322 N ALA B 406 25.090 35.025 24.733 1.00 24.99 B N ATOM 3323 CA ALA B 406 26.406 35.685 24.842 1.00 25.43 B C ATOM 3324 CB ALA B 406 27.508 34.778 24.318 1.00 25.46 B C ATOM 3325 C ALA B 406 26.431 37.010 24.086 1.00 28.22 B C ATOM 3326 O ALA B 406 27.327 37.839 24.272 1.00 27.95 B O ATOM 3327 N LEU B 407 25.448 37.197 23.217 1.00 24.41 B N ATOM 3328 CA LEU B 407 25.351 38.430 22.460 1.00 28.36 B C ATOM 3329 CB LEU B 407 24.969 38.132 21.011 1.00 27.77 B C ATOM 3330 CG LEU B 407 26.015 37.382 20.193 1.00 26.79 B C ATOM 3331 CD1 LEU B 407 25.579 37.346 18.731 1.00 23.59 B C ATOM 3332 CD2 LEU B 407 27.392 38.038 20.336 1.00 26.56 B C ATOM 3333 C LEU B 407 24.319 39.355 23.078 1.00 28.67 B C ATOM 3334 O LEU B 407 24.175 40.497 22.656 1.00 33.15 B O ATOM 3335 N GLY B 408 23.579 38.833 24.052 1.00 28.62 B N ATOM 3336 CA GLY B 408 22.600 39.622 24.777 1.00 30.08 B C ATOM 3337 C GLY B 408 21.142 39.282 24.523 1.00 30.37 B C ATOM 3338 O GLY B 408 20.283 40.100 24.837 1.00 28.46 B O ATOM 3339 N LEU B 409 20.848 38.100 23.969 1.00 26.51 B N ATOM 3340 CA LEU B 409 19.449 37.711 23.719 1.00 27.84 B C ATOM 3341 CB LEU B 409 19.311 36.884 22.438 1.00 27.28 B C ATOM 3342 CG LEU B 409 19.671 37.550 21.114 1.00 25.10 B C ATOM 3343 CD1 LEU B 409 19.694 36.481 20.019 1.00 25.82 B C ATOM 3344 CD2 LEU B 409 18.698 38.689 20.787 1.00 23.83 B C ATOM 3345 C LEU B 409 18.828 36.923 24.852 1.00 27.95 B C ATOM 3346 O LEU B 409 19.496 36.070 25.444 1.00 28.79 B O ATOM 3347 N ASP B 410 17.543 37.185 25.114 1.00 28.91 B N ATOM 3348 CA ASP B 410 16.740 36.418 26.086 1.00 30.81 B C ATOM 3349 CB ASP B 410 15.637 37.277 26.705 1.00 29.17 B C ATOM 3350 CG ASP B 410 16.174 38.494 27.414 1.00 38.66 B C ATOM 3351 OD1 ASP B 410 17.229 38.384 28.080 1.00 40.33 B O ATOM 3352 OD2 ASP B 410 15.536 39.566 27.317 1.00 45.38 B O ATOM 3353 C ASP B 410 16.059 35.277 25.367 1.00 32.04 B C ATOM 3354 O ASP B 410 16.233 35.099 24.165 1.00 28.03 B O ATOM 3355 N HIS B 411 15.248 34.518 26.087 1.00 26.05 B N ATOM 3356 CA HIS B 411 14.541 33.439 25.427 1.00 29.13 B C ATOM 3357 CB HIS B 411 14.105 32.352 26.409 1.00 33.92 B C ATOM 3358 CG HIS B 411 15.174 31.352 26.675 1.00 32.03 B C ATOM 3359 CD2 HIS B 411 16.406 31.204 26.119 1.00 30.56 B C ATOM 3360 ND1 HIS B 411 15.065 30.356 27.629 1.00 34.61 B N ATOM 3361 CE1 HIS B 411 16.179 29.641 27.638 1.00 33.82 B C ATOM 3362 NE2 HIS B 411 17.004 30.138 26.735 1.00 28.06 B N ATOM 3363 C HIS B 411 13.378 33.924 24.583 1.00 31.23 B C ATOM 3364 O HIS B 411 12.819 35.001 24.807 1.00 28.64 B O ATOM 3365 N SER B 412 13.055 33.114 23.585 1.00 31.15 B N ATOM 3366 CA SER B 412 11.911 33.352 22.734 1.00 30.15 B C ATOM 3367 CB SER B 412 12.273 32.994 21.295 1.00 27.70 B C ATOM 3368 OG SER B 412 11.135 33.102 20.475 1.00 24.43 B O ATOM 3369 C SER B 412 10.753 32.473 23.186 1.00 31.37 B C ATOM 3370 O SER B 412 10.966 31.356 23.656 1.00 29.87 B O ATOM 3371 N SER B 413 9.531 32.968 23.007 1.00 26.71 B N ATOM 3372 CA SER B 413 8.338 32.153 23.202 1.00 31.03 B C ATOM 3373 CB SER B 413 7.214 33.002 23.798 1.00 34.38 B C ATOM 3374 OG SER B 413 7.092 34.216 23.082 1.00 40.76 B O ATOM 3375 C SER B 413 7.855 31.468 21.913 1.00 32.05 B C ATOM 3376 O SER B 413 6.850 30.763 21.925 1.00 30.78 B O ATOM 3377 N VAL B 414 8.576 31.651 20.808 1.00 32.95 B N ATOM 3378 CA VAL B 414 8.260 30.929 19.567 1.00 29.80 B C ATOM 3379 CB VAL B 414 8.646 31.728 18.307 1.00 28.99 B C ATOM 3380 CG1 VAL B 414 8.342 30.928 17.032 1.00 32.17 B C ATOM 3381 CG2 VAL B 414 7.928 33.053 18.288 1.00 25.65 B C ATOM 3382 C VAL B 414 8.936 29.573 19.556 1.00 29.19 B C ATOM 3383 O VAL B 414 10.163 29.480 19.481 1.00 31.01 B O ATOM 3384 N PRO B 415 8.136 28.506 19.624 1.00 30.90 B N ATOM 3385 CD PRO B 415 6.665 28.520 19.734 1.00 35.68 B C ATOM 3386 CA PRO B 415 8.688 27.151 19.743 1.00 34.21 B C ATOM 3387 CB PRO B 415 7.455 26.260 19.613 1.00 34.44 B C ATOM 3388 CG PRO B 415 6.346 27.117 20.174 1.00 33.30 B C ATOM 3389 C PRO B 415 9.731 26.799 18.681 1.00 36.96 B C ATOM 3390 O PRO B 415 10.642 26.033 18.989 1.00 36.03 B O ATOM 3391 N GLU B 416 9.621 27.335 17.472 1.00 33.99 B N ATOM 3392 CA GLU B 416 10.605 26.978 16.440 1.00 36.21 B C ATOM 3393 CB GLU B 416 9.965 26.823 15.047 1.00 39.77 B C ATOM 3394 CG GLU B 416 8.764 27.722 14.784 1.00 44.91 B C ATOM 3395 CD GLU B 416 7.540 27.311 15.585 1.00 44.16 B C ATOM 3396 OE1 GLU B 416 7.320 26.092 15.768 1.00 46.86 B O ATOM 3397 OE2 GLU B 416 6.799 28.211 16.030 1.00 46.25 B O ATOM 3398 C GLU B 416 11.814 27.909 16.377 1.00 33.72 B C ATOM 3399 O GLU B 416 12.801 27.592 15.697 1.00 34.67 B O ATOM 3400 N ALA B 417 11.749 29.041 17.081 1.00 30.95 B N ATOM 3401 CA ALA B 417 12.873 29.981 17.100 1.00 32.49 B C ATOM 3402 CB ALA B 417 12.506 31.267 17.825 1.00 30.28 B C ATOM 3403 C ALA B 417 14.073 29.331 17.764 1.00 28.91 B C ATOM 3404 O ALA B 417 13.911 28.494 18.645 1.00 29.34 B O ATOM 3405 N LEU B 418 15.273 29.711 17.332 1.00 28.81 B N ATOM 3406 CA LEU B 418 16.503 29.209 17.940 1.00 26.35 B C ATOM 3407 CB LEU B 418 17.726 29.817 17.247 1.00 24.92 B C ATOM 3408 CG LEU B 418 19.110 29.453 17.785 1.00 25.05 B C ATOM 3409 CD1 LEU B 418 19.303 27.943 17.800 1.00 22.22 B C ATOM 3410 CD2 LEU B 418 20.215 30.131 16.971 1.00 24.84 B C ATOM 3411 C LEU B 418 16.574 29.502 19.446 1.00 25.86 B C ATOM 3412 O LEU B 418 17.052 28.677 20.224 1.00 22.75 B O ATOM 3413 N MET B 419 16.135 30.696 19.839 1.00 26.37 B N ATOM 3414 CA MET B 419 16.231 31.126 21.237 1.00 26.28 B C ATOM 3415 CB MET B 419 16.311 32.649 21.336 1.00 24.00 B C ATOM 3416 CG MET B 419 17.577 33.226 20.708 1.00 21.44 B C ATOM 3417 SD MET B 419 19.076 32.367 21.215 1.00 22.87 B S ATOM 3418 CE MET B 419 18.917 32.454 23.007 1.00 24.01 B C ATOM 3419 C MET B 419 15.104 30.567 22.121 1.00 28.16 B C ATOM 3420 O MET B 419 15.009 30.886 23.314 1.00 26.98 B O ATOM 3421 N TYR B 420 14.257 29.726 21.539 1.00 28.79 B N ATOM 3422 CA TYR B 420 13.312 28.959 22.344 1.00 28.91 B C ATOM 3423 CB TYR B 420 12.507 28.025 21.467 1.00 28.00 B C ATOM 3424 CG TYR B 420 11.261 27.502 22.142 1.00 31.87 B C ATOM 3425 CD1 TYR B 420 10.208 28.351 22.458 1.00 27.19 B C ATOM 3426 CE1 TYR B 420 9.065 27.868 23.062 1.00 35.06 B C ATOM 3427 CD2 TYR B 420 11.133 26.157 22.447 1.00 31.74 B C ATOM 3428 CE2 TYR B 420 10.002 25.667 23.054 1.00 34.36 B C ATOM 3429 CZ TYR B 420 8.974 26.519 23.354 1.00 34.05 B C ATOM 3430 OH TYR B 420 7.861 26.011 23.951 1.00 40.79 B O ATOM 3431 C TYR B 420 14.135 28.148 23.324 1.00 29.44 B C ATOM 3432 O TYR B 420 15.106 27.509 22.928 1.00 28.98 B O ATOM 3433 N PRO B 421 13.766 28.182 24.615 1.00 33.20 B N ATOM 3434 CD PRO B 421 12.658 28.983 25.162 1.00 30.72 B C ATOM 3435 CA PRO B 421 14.518 27.509 25.685 1.00 30.59 B C ATOM 3436 CB PRO B 421 13.665 27.791 26.936 1.00 30.50 B C ATOM 3437 CG PRO B 421 12.325 28.240 26.411 1.00 32.68 B C ATOM 3438 C PRO B 421 14.667 25.993 25.533 1.00 30.03 B C ATOM 3439 O PRO B 421 15.673 25.453 25.974 1.00 27.93 B O ATOM 3440 N MET B 422 13.676 25.309 24.973 1.00 29.71 B N ATOM 3441 CA MET B 422 13.721 23.849 24.941 1.00 28.60 B C ATOM 3442 CB MET B 422 12.332 23.258 24.728 1.00 32.16 B C ATOM 3443 CG MET B 422 11.365 23.451 25.872 1.00 36.01 B C ATOM 3444 SD MET B 422 9.923 22.435 25.550 1.00 42.48 B S ATOM 3445 CE MET B 422 8.632 23.501 26.177 1.00 36.39 B C ATOM 3446 C MET B 422 14.592 23.390 23.813 1.00 31.30 B C ATOM 3447 O MET B 422 14.645 24.042 22.779 1.00 30.45 B O ATOM 3448 N TYR B 423 15.270 22.264 24.011 1.00 34.86 B N ATOM 3449 CA TYR B 423 16.026 21.644 22.938 1.00 30.71 B C ATOM 3450 CB TYR B 423 16.916 20.519 23.450 1.00 32.97 B C ATOM 3451 CG TYR B 423 17.697 19.851 22.337 1.00 30.50 B C ATOM 3452 CD1 TYR B 423 17.351 18.583 21.872 1.00 32.84 B C ATOM 3453 CE1 TYR B 423 18.070 17.970 20.838 1.00 29.38 B C ATOM 3454 CD2 TYR B 423 18.757 20.503 21.724 1.00 31.81 B C ATOM 3455 CE2 TYR B 423 19.473 19.909 20.684 1.00 29.92 B C ATOM 3456 CZ TYR B 423 19.130 18.648 20.250 1.00 31.11 B C ATOM 3457 OH TYR B 423 19.854 18.061 19.237 1.00 26.55 B O ATOM 3458 C TYR B 423 15.053 21.068 21.933 1.00 35.03 B C ATOM 3459 O TYR B 423 14.051 20.457 22.304 1.00 31.33 B O ATOM 3460 N ARG B 424 15.350 21.272 20.657 1.00 33.05 B N ATOM 3461 CA ARG B 424 14.511 20.760 19.591 1.00 33.16 B C ATOM 3462 CB ARG B 424 13.358 21.725 19.300 1.00 35.92 B C ATOM 3463 CG ARG B 424 12.530 21.327 18.091 1.00 39.58 B C ATOM 3464 CD ARG B 424 11.908 22.537 17.387 1.00 48.60 B C ATOM 3465 NE ARG B 424 12.880 23.347 16.640 1.00 45.15 B N ATOM 3466 CZ ARG B 424 12.726 23.701 15.366 1.00 49.86 B C ATOM 3467 NH1 ARG B 424 11.646 23.303 14.696 1.00 50.15 B N ATOM 3468 NH2 ARG B 424 13.646 24.451 14.753 1.00 48.73 B N ATOM 3469 C ARG B 424 15.383 20.591 18.356 1.00 34.45 B C ATOM 3470 O ARG B 424 15.770 21.576 17.727 1.00 33.91 B O ATOM 3471 N PHE B 425 15.704 19.345 18.017 1.00 28.87 B N ATOM 3472 CA PHE B 425 16.628 19.105 16.919 1.00 33.27 B C ATOM 3473 CB PHE B 425 17.119 17.663 16.916 1.00 29.57 B C ATOM 3474 CG PHE B 425 17.965 17.338 15.738 1.00 34.93 B C ATOM 3475 CD1 PHE B 425 19.295 17.727 15.700 1.00 34.03 B C ATOM 3476 CD2 PHE B 425 17.426 16.676 14.639 1.00 36.58 B C ATOM 3477 CE1 PHE B 425 20.078 17.451 14.584 1.00 39.42 B C ATOM 3478 CE2 PHE B 425 18.211 16.392 13.520 1.00 35.31 B C ATOM 3479 CZ PHE B 425 19.535 16.781 13.499 1.00 39.08 B C ATOM 3480 C PHE B 425 16.012 19.470 15.562 1.00 34.13 B C ATOM 3481 O PHE B 425 14.815 19.316 15.346 1.00 29.55 B O ATOM 3482 N THR B 426 16.838 19.972 14.657 1.00 33.63 B N ATOM 3483 CA THR B 426 16.377 20.304 13.314 1.00 34.53 B C ATOM 3484 CB THR B 426 15.741 21.715 13.263 1.00 34.39 B C ATOM 3485 OG1 THR B 426 15.209 21.964 11.953 1.00 31.61 B O ATOM 3486 CG2 THR B 426 16.768 22.796 13.635 1.00 29.09 B C ATOM 3487 C THR B 426 17.528 20.203 12.325 1.00 34.34 B C ATOM 3488 O THR B 426 18.688 20.384 12.702 1.00 30.85 B O ATOM 3489 N GLU B 427 17.208 19.885 11.068 1.00 38.18 B N ATOM 3490 CA GLU B 427 18.199 19.886 9.992 1.00 35.10 B C ATOM 3491 CB GLU B 427 18.016 18.683 9.066 1.00 44.11 B C ATOM 3492 CG GLU B 427 18.074 17.335 9.772 1.00 47.56 B C ATOM 3493 CD GLU B 427 19.021 16.355 9.097 1.00 53.94 B C ATOM 3494 OE1 GLU B 427 20.241 16.630 9.045 1.00 57.20 B O ATOM 3495 OE2 GLU B 427 18.545 15.304 8.623 1.00 61.87 B O ATOM 3496 C GLU B 427 18.084 21.166 9.181 1.00 35.94 B C ATOM 3497 O GLU B 427 18.903 21.432 8.285 1.00 34.79 B O ATOM 3498 N GLY B 428 17.053 21.953 9.484 1.00 31.88 B N ATOM 3499 CA GLY B 428 16.831 23.212 8.797 1.00 32.26 B C ATOM 3500 C GLY B 428 17.721 24.347 9.281 1.00 31.02 B C ATOM 3501 O GLY B 428 18.388 24.227 10.314 1.00 29.01 B O ATOM 3502 N PRO B 429 17.731 25.466 8.541 1.00 28.00 B N ATOM 3503 CD PRO B 429 17.036 25.694 7.259 1.00 28.13 B C ATOM 3504 CA PRO B 429 18.463 26.652 9.001 1.00 24.79 B C ATOM 3505 CB PRO B 429 18.006 27.732 8.034 1.00 21.89 B C ATOM 3506 CG PRO B 429 17.687 26.944 6.745 1.00 27.05 B C ATOM 3507 C PRO B 429 18.045 27.006 10.430 1.00 22.34 B C ATOM 3508 O PRO B 429 16.851 27.123 10.689 1.00 22.46 B O ATOM 3509 N PRO B 430 19.012 27.184 11.343 1.00 22.20 B N ATOM 3510 CD PRO B 430 20.471 26.972 11.196 1.00 21.29 B C ATOM 3511 CA PRO B 430 18.586 27.379 12.747 1.00 24.42 B C ATOM 3512 CB PRO B 430 19.892 27.242 13.557 1.00 20.22 B C ATOM 3513 CG PRO B 430 20.894 26.505 12.572 1.00 22.79 B C ATOM 3514 C PRO B 430 17.891 28.718 13.020 1.00 23.73 B C ATOM 3515 O PRO B 430 16.994 28.727 13.841 1.00 25.76 B O ATOM 3516 N LEU B 431 18.259 29.816 12.363 1.00 20.50 B N ATOM 3517 CA LEU B 431 17.653 31.106 12.705 1.00 22.28 B C ATOM 3518 CB LEU B 431 18.480 32.290 12.191 1.00 24.19 B C ATOM 3519 CG LEU B 431 19.945 32.411 12.638 1.00 29.39 B C ATOM 3520 CD1 LEU B 431 20.636 33.593 11.971 1.00 20.80 B C ATOM 3521 CD2 LEU B 431 20.016 32.542 14.144 1.00 21.09 B C ATOM 3522 C LEU B 431 16.231 31.235 12.158 1.00 29.53 B C ATOM 3523 O LEU B 431 15.957 30.845 11.020 1.00 28.39 B O ATOM 3524 N HIS B 432 15.349 31.817 12.968 1.00 25.81 B N ATOM 3525 CA HIS B 432 14.011 32.189 12.542 1.00 24.87 B C ATOM 3526 CB HIS B 432 12.975 31.405 13.350 1.00 28.63 B C ATOM 3527 CG HIS B 432 12.981 29.943 13.032 1.00 29.15 B C ATOM 3528 CD2 HIS B 432 12.096 29.170 12.367 1.00 27.14 B C ATOM 3529 ND1 HIS B 432 14.041 29.119 13.361 1.00 34.09 B N ATOM 3530 CE1 HIS B 432 13.789 27.894 12.935 1.00 31.79 B C ATOM 3531 NE2 HIS B 432 12.619 27.899 12.323 1.00 29.89 B N ATOM 3532 C HIS B 432 13.826 33.695 12.639 1.00 24.60 B C ATOM 3533 O HIS B 432 14.700 34.395 13.160 1.00 25.43 B O ATOM 3534 N LYS B 433 12.719 34.195 12.092 1.00 26.75 B N ATOM 3535 CA LYS B 433 12.449 35.633 12.069 1.00 24.46 B C ATOM 3536 CB LYS B 433 11.038 35.897 11.550 1.00 30.73 B C ATOM 3537 CG LYS B 433 10.808 35.658 10.068 1.00 26.94 B C ATOM 3538 CD LYS B 433 9.301 35.741 9.777 1.00 34.47 B C ATOM 3539 CE LYS B 433 8.990 35.459 8.307 1.00 31.01 B C ATOM 3540 NZ LYS B 433 9.534 36.551 7.443 1.00 28.86 B N ATOM 3541 C LYS B 433 12.580 36.245 13.467 1.00 26.90 B C ATOM 3542 O LYS B 433 13.096 37.347 13.625 1.00 27.29 B O ATOM 3543 N ASP B 434 12.116 35.524 14.484 1.00 25.77 B N ATOM 3544 CA ASP B 434 12.135 36.061 15.856 1.00 25.26 B C ATOM 3545 CB ASP B 434 11.363 35.174 16.829 1.00 22.07 B C ATOM 3546 CG ASP B 434 11.123 35.869 18.167 1.00 26.22 B C ATOM 3547 OD1 ASP B 434 10.510 36.958 18.162 1.00 23.93 B O ATOM 3548 OD2 ASP B 434 11.590 35.349 19.201 1.00 22.23 B O ATOM 3549 C ASP B 434 13.546 36.281 16.376 1.00 24.03 B C ATOM 3550 O ASP B 434 13.819 37.290 17.016 1.00 25.85 B O ATOM 3551 N ASP B 435 14.436 35.334 16.087 1.00 25.46 B N ATOM 3552 CA ASP B 435 15.846 35.428 16.458 1.00 23.99 B C ATOM 3553 CB ASP B 435 16.582 34.166 15.999 1.00 25.35 B C ATOM 3554 CG ASP B 435 15.922 32.885 16.498 1.00 30.42 B C ATOM 3555 OD1 ASP B 435 15.716 32.758 17.722 1.00 25.09 B O ATOM 3556 OD2 ASP B 435 15.602 32.015 15.663 1.00 26.77 B O ATOM 3557 C ASP B 435 16.497 36.645 15.824 1.00 24.01 B C ATOM 3558 O ASP B 435 17.255 37.356 16.475 1.00 25.34 B O ATOM 3559 N VAL B 436 16.211 36.859 14.542 1.00 25.85 B N ATOM 3560 CA VAL B 436 16.793 37.966 13.772 1.00 26.06 B C ATOM 3561 CB VAL B 436 16.571 37.782 12.238 1.00 27.51 B C ATOM 3562 CG1 VAL B 436 17.201 38.941 11.445 1.00 27.33 B C ATOM 3563 CG2 VAL B 436 17.158 36.451 11.766 1.00 27.17 B C ATOM 3564 C VAL B 436 16.235 39.320 14.240 1.00 29.15 B C ATOM 3565 O VAL B 436 16.995 40.286 14.407 1.00 28.58 B O ATOM 3566 N ASN B 437 14.914 39.387 14.444 1.00 26.57 B N ATOM 3567 CA ASN B 437 14.293 40.585 15.020 1.00 29.07 B C ATOM 3568 CB ASN B 437 12.796 40.372 15.294 1.00 28.34 B C ATOM 3569 CG ASN B 437 11.974 40.208 14.019 1.00 33.61 B C ATOM 3570 OD1 ASN B 437 12.366 40.679 12.949 1.00 32.14 B O ATOM 3571 ND2 ASN B 437 10.823 39.536 14.132 1.00 30.32 B N ATOM 3572 C ASN B 437 15.001 40.955 16.316 1.00 25.22 B C ATOM 3573 O ASN B 437 15.465 42.078 16.495 1.00 28.31 B O ATOM 3574 N GLY B 438 15.122 39.981 17.199 1.00 24.42 B N ATOM 3575 CA GLY B 438 15.808 40.189 18.463 1.00 27.50 B C ATOM 3576 C GLY B 438 17.217 40.728 18.329 1.00 28.51 B C ATOM 3577 O GLY B 438 17.596 41.698 18.981 1.00 27.54 B O ATOM 3578 N ILE B 439 18.018 40.096 17.486 1.00 26.65 B N ATOM 3579 CA ILE B 439 19.408 40.484 17.420 1.00 26.26 B C ATOM 3580 CB ILE B 439 20.273 39.432 16.674 1.00 26.21 B C ATOM 3581 CG2 ILE B 439 20.083 39.535 15.161 1.00 25.28 B C ATOM 3582 CG1 ILE B 439 21.747 39.555 17.081 1.00 24.32 B C ATOM 3583 CD1 ILE B 439 21.980 39.393 18.563 1.00 26.87 B C ATOM 3584 C ILE B 439 19.498 41.885 16.794 1.00 30.94 B C ATOM 3585 O ILE B 439 20.248 42.742 17.265 1.00 30.45 B O ATOM 3586 N ARG B 440 18.696 42.128 15.766 1.00 26.81 B N ATOM 3587 CA ARG B 440 18.649 43.449 15.147 1.00 30.84 B C ATOM 3588 CB ARG B 440 17.696 43.437 13.961 1.00 30.25 B C ATOM 3589 CG ARG B 440 18.273 42.741 12.762 1.00 33.60 B C ATOM 3590 CD ARG B 440 17.303 42.728 11.595 1.00 37.68 B C ATOM 3591 NE ARG B 440 17.919 42.074 10.451 1.00 35.24 B N ATOM 3592 CZ ARG B 440 17.278 41.727 9.340 1.00 38.70 B C ATOM 3593 NH1 ARG B 440 15.976 41.973 9.206 1.00 36.90 B N ATOM 3594 NH2 ARG B 440 17.950 41.128 8.358 1.00 31.03 B N ATOM 3595 C ARG B 440 18.207 44.528 16.133 1.00 33.72 B C ATOM 3596 O ARG B 440 18.595 45.695 16.007 1.00 33.48 B O ATOM 3597 N HIS B 441 17.377 44.146 17.101 1.00 31.14 B N ATOM 3598 CA HIS B 441 16.892 45.111 18.085 1.00 32.92 B C ATOM 3599 CB HIS B 441 15.733 44.537 18.907 1.00 34.49 B C ATOM 3600 CG HIS B 441 15.268 45.445 20.003 1.00 45.53 B C ATOM 3601 CD2 HIS B 441 14.319 46.411 20.018 1.00 48.79 B C ATOM 3602 ND1 HIS B 441 15.817 45.428 21.271 1.00 46.98 B N ATOM 3603 CE1 HIS B 441 15.220 46.338 22.019 1.00 50.20 B C ATOM 3604 NE2 HIS B 441 14.301 46.946 21.285 1.00 51.16 B N ATOM 3605 C HIS B 441 18.041 45.529 18.995 1.00 38.57 B C ATOM 3606 O HIS B 441 18.026 46.615 19.571 1.00 40.14 B O ATOM 3607 N LEU B 442 19.046 44.660 19.103 1.00 32.63 B N ATOM 3608 CA LEU B 442 20.229 44.928 19.917 1.00 30.97 B C ATOM 3609 CB LEU B 442 20.781 43.623 20.488 1.00 28.63 B C ATOM 3610 CG LEU B 442 20.372 43.210 21.898 1.00 34.83 B C ATOM 3611 CD1 LEU B 442 18.883 43.388 22.080 1.00 36.94 B C ATOM 3612 CD2 LEU B 442 20.786 41.782 22.183 1.00 29.80 B C ATOM 3613 C LEU B 442 21.341 45.635 19.137 1.00 35.56 B C ATOM 3614 O LEU B 442 22.005 46.529 19.666 1.00 36.63 B O ATOM 3615 N TYR B 443 21.544 45.228 17.884 1.00 30.53 B N ATOM 3616 CA TYR B 443 22.701 45.667 17.114 1.00 32.78 B C ATOM 3617 CB TYR B 443 23.627 44.476 16.854 1.00 31.82 B C ATOM 3618 CG TYR B 443 24.198 43.893 18.124 1.00 29.74 B C ATOM 3619 CD1 TYR B 443 23.709 42.706 18.659 1.00 30.39 B C ATOM 3620 CE1 TYR B 443 24.240 42.177 19.839 1.00 27.91 B C ATOM 3621 CD2 TYR B 443 25.219 44.548 18.802 1.00 30.48 B C ATOM 3622 CE2 TYR B 443 25.752 44.037 19.968 1.00 30.86 B C ATOM 3623 CZ TYR B 443 25.260 42.859 20.488 1.00 29.82 B C ATOM 3624 OH TYR B 443 25.805 42.376 21.659 1.00 31.08 B O ATOM 3625 C TYR B 443 22.357 46.398 15.807 1.00 34.22 B C ATOM 3626 O TYR B 443 23.237 46.916 15.127 1.00 32.66 B O ATOM 3627 N GLY B 444 21.077 46.457 15.471 1.00 34.41 B N ATOM 3628 CA GLY B 444 20.648 47.198 14.300 1.00 31.44 B C ATOM 3629 C GLY B 444 20.413 46.304 13.097 1.00 31.12 B C ATOM 3630 O GLY B 444 19.615 46.666 12.230 1.00 35.92 B O ATOM 3631 ZN ZN B 500 18.910 29.703 26.678 1.00 27.12 B Zn ATOM 3632 ZN ZN B 501 28.355 27.403 34.053 1.00 34.65 B Zn ATOM 3633 CA CA B 502 22.163 18.142 32.164 1.00 39.48 B Ca ATOM 3634 CA CA B 504 33.559 36.767 29.256 1.00 47.51 B Ca ATOM 3635 CA CA B 505 32.672 45.975 25.669 1.00 44.27 B Ca TER 3636 CA B 505 ATOM 3637 C01 LIG C 1 24.110 30.449 33.901 1.00 34.08 A C ATOM 3638 O02 LIG C 1 23.352 31.511 33.335 1.00 36.24 A O ATOM 3639 C03 LIG C 1 22.501 32.268 34.080 1.00 40.44 A C ATOM 3640 C04 LIG C 1 22.146 31.902 35.391 1.00 42.42 A C ATOM 3641 C05 LIG C 1 21.275 32.763 36.114 1.00 47.88 A C ATOM 3642 N06 LIG C 1 20.815 33.897 35.556 1.00 46.45 A N ATOM 3643 C07 LIG C 1 21.172 34.235 34.287 1.00 41.20 A C ATOM 3644 C08 LIG C 1 22.041 33.467 33.454 1.00 42.18 A C ATOM 3645 N09 LIG C 1 22.379 33.897 32.063 1.00 35.32 A N ATOM 3646 C10 LIG C 1 21.935 34.914 31.145 1.00 32.60 A C ATOM 3647 N11 LIG C 1 21.214 36.003 31.535 1.00 34.30 A N ATOM 3648 C12 LIG C 1 20.852 36.958 30.444 1.00 34.71 A C ATOM 3649 C13 LIG C 1 21.346 36.484 29.224 1.00 33.87 A C ATOM 3650 C14 LIG C 1 21.188 37.139 27.983 1.00 32.44 A C ATOM 3651 C15 LIG C 1 20.479 38.352 27.896 1.00 36.08 A C ATOM 3652 C16 LIG C 1 19.947 38.903 29.089 1.00 35.28 A C ATOM 3653 C17 LIG C 1 20.112 38.250 30.340 1.00 32.01 A C ATOM 3654 N18 LIG C 1 19.466 39.070 31.289 1.00 35.21 A N ATOM 3655 C19 LIG C 1 18.911 40.190 30.667 1.00 34.92 A C ATOM 3656 N20 LIG C 1 19.218 40.103 29.259 1.00 36.38 A N ATOM 3657 C21 LIG C 1 18.734 41.214 28.408 1.00 32.86 A C ATOM 3658 S22 LIG C 1 22.226 34.937 29.381 1.00 33.80 A S TER 3659 LIG C 1 END

TABLE 15 Coordinates for apo form of proMMP9(35-444 ΔFnII) (SEQ ID NO: 12) ATOM 1 N THR A 40 4.483 62.393 28.469 1.00 40.90 A N ATOM 2 CA THR A 40 5.618 62.127 27.595 1.00 36.29 A C ATOM 3 C THR A 40 5.484 62.867 26.258 1.00 40.20 A C ATOM 4 CB THR A 40 5.833 60.616 27.364 1.00 37.71 A C ATOM 5 OG1 THR A 40 7.107 60.389 26.747 1.00 50.31 A O ATOM 6 CG2 THR A 40 4.734 60.029 26.479 1.00 45.76 A C ATOM 7 O THR A 40 6.491 63.196 25.628 1.00 37.63 A O ATOM 8 CB ASP A 41 2.518 64.003 24.285 1.00 34.93 A C ATOM 9 CG ASP A 41 2.131 62.918 23.300 1.00 31.19 A C ATOM 10 OD1 ASP A 41 3.028 62.258 22.743 1.00 26.69 A O ATOM 11 OD2 ASP A 41 0.918 62.729 23.073 1.00 41.82 A O ATOM 12 C ASP A 41 4.493 65.371 24.963 1.00 33.68 A C ATOM 13 O ASP A 41 5.296 65.925 24.212 1.00 29.75 A O ATOM 14 N ASP A 41 4.246 63.118 25.825 1.00 38.23 A N ATOM 15 CA ASP A 41 4.000 63.964 24.656 1.00 32.68 A C ATOM 16 N ARG A 42 4.038 65.931 26.083 1.00 31.38 A N ATOM 17 CA ARG A 42 4.503 67.242 26.511 1.00 34.49 A C ATOM 18 CB ARG A 42 3.591 67.845 27.590 1.00 31.03 A C ATOM 19 CG ARG A 42 3.781 69.351 27.770 1.00 46.76 A C ATOM 20 CD ARG A 42 3.426 69.828 29.177 1.00 49.89 A C ATOM 21 NE ARG A 42 4.144 71.051 29.539 1.00 47.62 A N ATOM 22 CZ ARG A 42 3.681 72.282 29.340 1.00 50.03 A C ATOM 23 NH1 ARG A 42 2.490 72.466 28.780 1.00 44.68 A N ATOM 24 NH2 ARG A 42 4.411 73.334 29.699 1.00 52.81 A N ATOM 25 C ARG A 42 5.950 67.164 26.995 1.00 33.54 A C ATOM 26 O ARG A 42 6.609 68.189 27.179 1.00 39.68 A O ATOM 27 N GLN A 43 6.450 65.946 27.165 1.00 30.55 A N ATOM 28 CA GLN A 43 7.819 65.733 27.610 1.00 31.28 A C ATOM 29 CB GLN A 43 7.954 64.351 28.241 1.00 35.35 A C ATOM 30 CG GLN A 43 9.378 63.942 28.602 1.00 34.39 A C ATOM 31 CD GLN A 43 9.451 62.551 29.232 1.00 43.96 A C ATOM 32 OE1 GLN A 43 8.458 61.815 29.268 1.00 48.25 A O ATOM 33 NE2 GLN A 43 10.631 62.186 29.728 1.00 37.47 A N ATOM 34 C GLN A 43 8.768 65.838 26.429 1.00 34.66 A C ATOM 35 O GLN A 43 9.805 66.506 26.495 1.00 25.95 A O ATOM 36 N LEU A 44 8.419 65.146 25.351 1.00 29.54 A N ATOM 37 CA LEU A 44 9.218 65.196 24.146 1.00 29.84 A C ATOM 38 CB LEU A 44 8.694 64.183 23.120 1.00 29.32 A C ATOM 39 CG LEU A 44 8.738 64.503 21.630 1.00 28.05 A C ATOM 40 CD1 LEU A 44 8.553 63.245 20.831 1.00 35.77 A C ATOM 41 CD2 LEU A 44 7.648 65.503 21.285 1.00 32.67 A C ATOM 42 C LEU A 44 9.247 66.633 23.619 1.00 27.22 A C ATOM 43 O LEU A 44 10.297 67.124 23.210 1.00 29.06 A O ATOM 44 N ALA A 45 8.106 67.313 23.684 1.00 22.68 A N ATOM 45 CA ALA A 45 7.982 68.678 23.175 1.00 22.75 A C ATOM 46 CB ALA A 45 6.540 69.090 23.124 1.00 24.95 A C ATOM 47 C ALA A 45 8.811 69.683 23.960 1.00 30.88 A C ATOM 48 O ALA A 45 9.348 70.651 23.404 1.00 27.08 A O ATOM 49 N GLU A 46 8.929 69.454 25.258 1.00 30.19 A N ATOM 50 CA GLU A 46 9.782 70.296 26.068 1.00 31.83 A C ATOM 51 CB GLU A 46 9.548 70.032 27.544 1.00 29.47 A C ATOM 52 CG GLU A 46 8.265 70.601 28.040 1.00 38.13 A C ATOM 53 CD GLU A 46 8.135 70.466 29.541 1.00 46.63 A C ATOM 54 OE1 GLU A 46 9.165 70.197 30.209 1.00 45.80 A O ATOM 55 OE2 GLU A 46 7.004 70.631 30.044 1.00 51.36 A O ATOM 56 C GLU A 46 11.245 70.082 25.741 1.00 29.61 A C ATOM 57 O GLU A 46 12.006 71.039 25.644 1.00 31.21 A O ATOM 58 N GLU A 47 11.636 68.825 25.583 1.00 28.18 A N ATOM 59 CA GLU A 47 13.024 68.495 25.296 1.00 27.62 A C ATOM 60 CB GLU A 47 13.270 67.002 25.551 1.00 30.67 A C ATOM 61 CG GLU A 47 14.678 66.510 25.234 1.00 38.26 A C ATOM 62 CD GLU A 47 15.740 67.068 26.188 1.00 46.31 A C ATOM 63 OE1 GLU A 47 15.510 67.060 27.421 1.00 47.56 A O ATOM 64 OE2 GLU A 47 16.810 67.507 25.701 1.00 41.49 A O ATOM 65 C GLU A 47 13.419 68.872 23.862 1.00 30.84 A C ATOM 66 O GLU A 47 14.592 69.133 23.571 1.00 30.11 A O ATOM 67 N TYR A 48 12.446 68.887 22.959 1.00 28.21 A N ATOM 68 CA TYR A 48 12.713 69.269 21.581 1.00 25.17 A C ATOM 69 CB TYR A 48 11.562 68.817 20.675 1.00 25.52 A C ATOM 70 CG TYR A 48 11.836 68.853 19.184 1.00 20.18 A C ATOM 71 CD1 TYR A 48 11.754 70.038 18.451 1.00 23.22 A C ATOM 72 CE1 TYR A 48 11.981 70.048 17.053 1.00 20.40 A C ATOM 73 CD2 TYR A 48 12.117 67.684 18.495 1.00 18.19 A C ATOM 74 CE2 TYR A 48 12.331 67.684 17.134 1.00 22.38 A C ATOM 75 CZ TYR A 48 12.281 68.869 16.410 1.00 20.91 A C ATOM 76 OH TYR A 48 12.501 68.817 15.036 1.00 19.25 A O ATOM 77 C TYR A 48 12.871 70.778 21.507 1.00 25.72 A C ATOM 78 O TYR A 48 13.844 71.299 20.944 1.00 23.40 A O ATOM 79 N LEU A 49 11.898 71.482 22.067 1.00 25.98 A N ATOM 80 CA LEU A 49 11.923 72.927 22.043 1.00 24.08 A C ATOM 81 CB LEU A 49 10.672 73.494 22.710 1.00 29.21 A C ATOM 82 CG LEU A 49 9.377 73.249 21.937 1.00 28.10 A C ATOM 83 CD1 LEU A 49 8.170 73.560 22.819 1.00 22.99 A C ATOM 84 CD2 LEU A 49 9.366 74.093 20.665 1.00 22.02 A C ATOM 85 C LEU A 49 13.176 73.441 22.720 1.00 25.30 A C ATOM 86 O LEU A 49 13.756 74.437 22.298 1.00 24.37 A O ATOM 87 N TYR A 50 13.594 72.771 23.785 1.00 32.10 A N ATOM 88 CA TYR A 50 14.774 73.222 24.498 1.00 29.27 A C ATOM 89 CB TYR A 50 14.887 72.579 25.877 1.00 27.89 A C ATOM 90 CG TYR A 50 16.308 72.587 26.375 1.00 28.86 A C ATOM 91 CD1 TYR A 50 16.845 73.720 26.983 1.00 34.49 A C ATOM 92 CE1 TYR A 50 18.158 73.741 27.419 1.00 30.57 A C ATOM 93 CD2 TYR A 50 17.132 71.484 26.196 1.00 26.45 A C ATOM 94 CE2 TYR A 50 18.450 71.496 26.632 1.00 32.25 A C ATOM 95 CZ TYR A 50 18.953 72.627 27.245 1.00 30.20 A C ATOM 96 OH TYR A 50 20.258 72.645 27.674 1.00 39.22 A O ATOM 97 C TYR A 50 16.030 72.929 23.710 1.00 26.53 A C ATOM 98 O TYR A 50 16.894 73.789 23.571 1.00 25.74 A O ATOM 99 N ARG A 51 16.115 71.705 23.195 1.00 23.80 A N ATOM 100 CA ARG A 51 17.332 71.199 22.598 1.00 25.93 A C ATOM 101 CB ARG A 51 17.181 69.698 22.315 1.00 24.27 A C ATOM 102 CG ARG A 51 18.402 69.017 21.768 1.00 28.40 A C ATOM 103 CD ARG A 51 18.058 67.675 21.116 1.00 25.29 A C ATOM 104 NE ARG A 51 18.224 66.552 22.031 1.00 23.90 A N ATOM 105 CZ ARG A 51 19.401 66.032 22.365 1.00 30.22 A C ATOM 106 NH1 ARG A 51 20.526 66.542 21.859 1.00 24.09 A N ATOM 107 NH2 ARG A 51 19.455 65.012 23.217 1.00 28.39 A N ATOM 108 C ARG A 51 17.651 71.974 21.317 1.00 24.58 A C ATOM 109 O ARG A 51 18.804 72.207 20.991 1.00 22.58 A O ATOM 110 N TYR A 52 16.620 72.396 20.599 1.00 24.72 A N ATOM 111 CA TYR A 52 16.851 73.005 19.300 1.00 20.25 A C ATOM 112 CB TYR A 52 15.935 72.375 18.252 1.00 17.52 A C ATOM 113 CG TYR A 52 16.246 70.910 18.046 1.00 22.29 A C ATOM 114 CD1 TYR A 52 15.281 69.933 18.239 1.00 22.95 A C ATOM 115 CE1 TYR A 52 15.583 68.587 18.066 1.00 21.99 A C ATOM 116 CD2 TYR A 52 17.527 70.504 17.672 1.00 20.02 A C ATOM 117 CE2 TYR A 52 17.831 69.172 17.480 1.00 24.00 A C ATOM 118 CZ TYR A 52 16.857 68.222 17.677 1.00 20.03 A C ATOM 119 OH TYR A 52 17.163 66.903 17.492 1.00 24.36 A O ATOM 120 C TYR A 52 16.787 74.533 19.334 1.00 22.92 A C ATOM 121 O TYR A 52 16.763 75.195 18.290 1.00 25.08 A O ATOM 122 N GLY A 53 16.786 75.081 20.550 1.00 24.92 A N ATOM 123 CA GLY A 53 16.982 76.505 20.762 1.00 24.54 A C ATOM 124 C GLY A 53 15.734 77.342 20.950 1.00 24.30 A C ATOM 125 O GLY A 53 15.818 78.510 21.302 1.00 29.51 A O ATOM 126 N TYR A 54 14.570 76.752 20.728 1.00 25.19 A N ATOM 127 CA TYR A 54 13.324 77.519 20.682 1.00 22.92 A C ATOM 128 CB TYR A 54 12.204 76.652 20.136 1.00 26.90 A C ATOM 129 CG TYR A 54 12.432 76.241 18.709 1.00 24.65 A C ATOM 130 CD1 TYR A 54 12.849 74.954 18.397 1.00 25.06 A C ATOM 131 CE1 TYR A 54 13.063 74.574 17.088 1.00 21.40 A C ATOM 132 CD2 TYR A 54 12.253 77.151 17.674 1.00 21.87 A C ATOM 133 CE2 TYR A 54 12.469 76.783 16.360 1.00 19.39 A C ATOM 134 CZ TYR A 54 12.875 75.492 16.079 1.00 21.02 A C ATOM 135 OH TYR A 54 13.093 75.116 14.778 1.00 17.04 A O ATOM 136 C TYR A 54 12.894 78.111 22.021 1.00 24.21 A C ATOM 137 O TYR A 54 12.323 79.187 22.064 1.00 27.10 A O ATOM 138 N THR A 55 13.142 77.399 23.109 1.00 27.82 A N ATOM 139 CA THR A 55 12.651 77.860 24.406 1.00 31.86 A C ATOM 140 CB THR A 55 12.746 76.760 25.481 1.00 32.13 A C ATOM 141 OG1 THR A 55 14.120 76.495 25.783 1.00 39.86 A O ATOM 142 CG2 THR A 55 12.098 75.489 25.001 1.00 25.96 A C ATOM 143 C THR A 55 13.450 79.079 24.848 1.00 33.75 A C ATOM 144 O THR A 55 12.886 80.098 25.262 1.00 33.26 A O ATOM 145 N ARG A 56 14.771 78.968 24.738 1.00 32.93 A N ATOM 146 CA ARG A 56 15.676 80.054 25.085 1.00 30.97 A C ATOM 147 CB ARG A 56 17.114 79.641 24.766 1.00 33.53 A C ATOM 148 CG ARG A 56 18.149 80.659 25.186 1.00 35.77 A C ATOM 149 CD ARG A 56 17.908 81.157 26.608 1.00 31.00 A C ATOM 150 NE ARG A 56 18.586 82.431 26.815 1.00 32.41 A N ATOM 151 CZ ARG A 56 18.158 83.405 27.611 1.00 33.08 A C ATOM 152 NH1 ARG A 56 17.037 83.263 28.305 1.00 33.98 A N ATOM 153 NH2 ARG A 56 18.859 84.529 27.706 1.00 32.57 A N ATOM 154 C ARG A 56 15.308 81.326 24.322 1.00 33.59 A C ATOM 155 O ARG A 56 15.260 82.419 24.876 1.00 31.90 A O ATOM 156 N VAL A 57 15.041 81.175 23.036 1.00 31.11 A N ATOM 157 CA VAL A 57 14.621 82.309 22.222 1.00 31.66 A C ATOM 158 CB VAL A 57 14.572 81.920 20.735 1.00 26.54 A C ATOM 159 CG1 VAL A 57 14.095 83.089 19.881 1.00 30.64 A C ATOM 160 CG2 VAL A 57 15.950 81.457 20.288 1.00 32.62 A C ATOM 161 C VAL A 57 13.274 82.856 22.690 1.00 30.02 A C ATOM 162 O VAL A 57 13.071 84.069 22.738 1.00 29.28 A O ATOM 163 N GLY A 58 12.353 81.961 23.036 1.00 26.98 A N ATOM 164 CA GLY A 58 11.062 82.364 23.568 1.00 29.77 A C ATOM 165 C GLY A 58 11.222 83.166 24.852 1.00 32.88 A C ATOM 166 O GLY A 58 10.517 84.150 25.086 1.00 34.39 A O ATOM 167 N GLU A 59 12.162 82.736 25.689 1.00 34.03 A N ATOM 168 CA GLU A 59 12.502 83.455 26.914 1.00 35.29 A C ATOM 169 C GLU A 59 13.006 84.860 26.623 1.00 34.85 A C ATOM 170 CB GLU A 59 13.569 82.697 27.692 1.00 33.35 A C ATOM 171 CG GLU A 59 13.140 81.327 28.148 1.00 41.75 A C ATOM 172 CD GLU A 59 14.127 80.706 29.113 1.00 44.85 A C ATOM 173 OE1 GLU A 59 15.233 81.273 29.285 1.00 40.01 A O ATOM 174 OE2 GLU A 59 13.793 79.654 29.699 1.00 43.89 A O ATOM 175 O GLU A 59 12.522 85.830 27.209 1.00 32.29 A O ATOM 176 N MET A 60 13.982 84.960 25.716 1.00 35.10 A N ATOM 177 CA MET A 60 14.541 86.246 25.285 1.00 30.26 A C ATOM 178 C MET A 60 13.464 87.213 24.802 1.00 28.22 A C ATOM 179 CB MET A 60 15.574 86.056 24.158 1.00 23.03 A C ATOM 180 CG MET A 60 16.825 85.292 24.548 1.00 29.72 A C ATOM 181 SD MET A 60 17.965 85.001 23.171 1.00 38.67 A S ATOM 182 CE MET A 60 18.982 83.719 23.890 1.00 36.29 A C ATOM 183 O MET A 60 13.692 88.418 24.729 1.00 29.93 A O ATOM 184 N ARG A 61 12.298 86.692 24.447 1.00 31.47 A N ATOM 185 CA ARG A 61 11.228 87.556 23.959 1.00 30.85 A C ATOM 186 C ARG A 61 10.194 87.835 25.036 1.00 32.84 A C ATOM 187 CB ARG A 61 10.571 86.959 22.720 1.00 35.78 A C ATOM 188 CG ARG A 61 11.559 86.625 21.608 1.00 36.76 A C ATOM 189 CD ARG A 61 10.834 86.421 20.297 1.00 43.82 A C ATOM 190 NE ARG A 61 11.733 86.024 19.221 1.00 45.48 A N ATOM 191 CZ ARG A 61 11.376 85.985 17.943 1.00 45.71 A C ATOM 192 NH1 ARG A 61 12.249 85.612 17.019 1.00 43.23 A N ATOM 193 NH2 ARG A 61 10.139 86.322 17.593 1.00 50.16 A N ATOM 194 O ARG A 61 9.127 88.392 24.751 1.00 41.35 A O ATOM 195 N GLY A 62 10.523 87.445 26.268 1.00 34.73 A N ATOM 196 CA GLY A 62 9.660 87.656 27.421 1.00 36.71 A C ATOM 197 C GLY A 62 8.474 86.701 27.440 1.00 45.80 A C ATOM 198 O GLY A 62 7.471 86.933 28.137 1.00 31.18 A O ATOM 199 N GLU A 63 8.597 85.631 26.656 1.00 38.06 A N ATOM 200 CA GLU A 63 7.580 84.594 26.572 1.00 44.09 A C ATOM 201 C GLU A 63 8.126 83.266 27.104 1.00 51.66 A C ATOM 202 CB GLU A 63 7.091 84.450 25.128 1.00 40.71 A C ATOM 203 CG GLU A 63 6.637 85.778 24.515 1.00 43.80 A C ATOM 204 CD GLU A 63 6.009 85.628 23.138 1.00 49.57 A C ATOM 205 OE1 GLU A 63 6.567 86.184 22.166 1.00 46.80 A O ATOM 206 OE2 GLU A 63 4.953 84.963 23.024 1.00 51.70 A O ATOM 207 O GLU A 63 8.194 82.266 26.378 1.00 44.27 A O ATOM 208 N SER A 64 8.530 83.273 28.376 1.00 52.59 A N ATOM 209 CA SER A 64 8.997 82.063 29.055 1.00 51.91 A C ATOM 210 C SER A 64 7.817 81.467 29.807 1.00 56.18 A C ATOM 211 CB SER A 64 10.161 82.374 30.004 1.00 51.80 A C ATOM 212 OG SER A 64 9.914 83.555 30.757 1.00 57.31 A O ATOM 213 O SER A 64 7.962 80.600 30.673 1.00 56.45 A O ATOM 214 N LYS A 65 6.641 81.962 29.448 1.00 55.59 A N ATOM 215 CA LYS A 65 5.382 81.514 30.007 1.00 52.13 A C ATOM 216 C LYS A 65 5.177 80.029 29.710 1.00 51.19 A C ATOM 217 CB LYS A 65 4.265 82.330 29.361 1.00 50.23 A C ATOM 218 CG LYS A 65 4.317 82.257 27.839 1.00 47.29 A C ATOM 219 CD LYS A 65 3.363 83.215 27.181 1.00 49.48 A C ATOM 220 CE LYS A 65 4.017 84.562 26.957 1.00 45.84 A C ATOM 221 NZ LYS A 65 3.033 85.498 26.366 1.00 49.66 A N ATOM 222 O LYS A 65 5.910 79.179 30.211 1.00 54.91 A O ATOM 223 N SER A 66 4.178 79.733 28.880 1.00 48.71 A N ATOM 224 CA SER A 66 3.850 78.371 28.480 1.00 40.20 A C ATOM 225 C SER A 66 4.672 77.907 27.276 1.00 44.34 A C ATOM 226 CB SER A 66 2.361 78.275 28.144 1.00 39.36 A C ATOM 227 OG SER A 66 2.087 78.785 26.851 1.00 34.18 A O ATOM 228 O SER A 66 5.731 78.457 26.973 1.00 40.20 A O ATOM 229 N LEU A 67 4.164 76.889 26.592 1.00 33.76 A N ATOM 230 CA LEU A 67 4.824 76.313 25.432 1.00 35.53 A C ATOM 231 C LEU A 67 4.461 77.043 24.135 1.00 31.78 A C ATOM 232 CB LEU A 67 4.421 74.839 25.310 1.00 31.23 A C ATOM 233 CG LEU A 67 5.468 73.743 25.499 1.00 33.63 A C ATOM 234 CD1 LEU A 67 6.291 73.951 26.746 1.00 33.37 A C ATOM 235 CD2 LEU A 67 4.763 72.392 25.534 1.00 34.78 A C ATOM 236 O LEU A 67 5.205 76.995 23.152 1.00 31.32 A O ATOM 237 N GLY A 68 3.314 77.711 24.134 1.00 31.62 A N ATOM 238 CA GLY A 68 2.761 78.287 22.917 1.00 29.84 A C ATOM 239 C GLY A 68 3.694 79.115 22.047 1.00 29.31 A C ATOM 240 O GLY A 68 3.815 78.873 20.849 1.00 33.24 A O ATOM 241 N PRO A 69 4.351 80.115 22.638 1.00 34.73 A N ATOM 242 CD PRO A 69 4.232 80.539 24.040 1.00 31.89 A C ATOM 243 CA PRO A 69 5.248 80.985 21.868 1.00 31.91 A C ATOM 244 CB PRO A 69 5.774 81.966 22.919 1.00 37.73 A C ATOM 245 CG PRO A 69 4.731 81.948 23.994 1.00 38.02 A C ATOM 246 C PRO A 69 6.405 80.221 21.229 1.00 28.12 A C ATOM 247 O PRO A 69 6.737 80.486 20.067 1.00 28.21 A O ATOM 248 N ALA A 70 6.986 79.281 21.968 1.00 31.12 A N ATOM 249 CA ALA A 70 8.093 78.460 21.479 1.00 26.40 A C ATOM 250 CB ALA A 70 8.701 77.662 22.626 1.00 22.85 A C ATOM 251 C ALA A 70 7.660 77.512 20.363 1.00 28.06 A C ATOM 252 O ALA A 70 8.433 77.226 19.442 1.00 25.01 A O ATOM 253 N LEU A 71 6.425 77.024 20.443 1.00 26.95 A N ATOM 254 CA LEU A 71 5.882 76.165 19.403 1.00 24.95 A C ATOM 255 CB LEU A 71 4.580 75.509 19.865 1.00 28.51 A C ATOM 256 CG LEU A 71 4.649 74.454 20.967 1.00 21.74 A C ATOM 257 CD1 LEU A 71 3.252 74.226 21.480 1.00 24.96 A C ATOM 258 CD2 LEU A 71 5.263 73.141 20.483 1.00 28.93 A C ATOM 259 C LEU A 71 5.643 76.954 18.115 1.00 26.22 A C ATOM 260 O LEU A 71 5.836 76.432 17.014 1.00 27.53 A O ATOM 261 N LEU A 72 5.213 78.206 18.249 1.00 22.00 A N ATOM 262 CA LEU A 72 5.059 79.084 17.084 1.00 27.23 A C ATOM 263 CB LEU A 72 4.465 80.434 17.485 1.00 27.24 A C ATOM 264 CG LEU A 72 3.816 81.234 16.354 1.00 34.35 A C ATOM 265 CD1 LEU A 72 2.577 80.523 15.831 1.00 31.76 A C ATOM 266 CD2 LEU A 72 3.464 82.643 16.821 1.00 36.81 A C ATOM 267 C LEU A 72 6.393 79.313 16.375 1.00 25.92 A C ATOM 268 O LEU A 72 6.478 79.272 15.146 1.00 24.25 A O ATOM 269 N LEU A 73 7.434 79.565 17.159 1.00 27.76 A N ATOM 270 CA LEU A 73 8.762 79.750 16.594 1.00 27.24 A C ATOM 271 CB LEU A 73 9.770 80.064 17.693 1.00 30.21 A C ATOM 272 CG LEU A 73 9.709 81.473 18.277 1.00 31.62 A C ATOM 273 CD1 LEU A 73 10.776 81.651 19.341 1.00 30.89 A C ATOM 274 CD2 LEU A 73 9.852 82.503 17.175 1.00 32.28 A C ATOM 275 C LEU A 73 9.199 78.508 15.831 1.00 25.05 A C ATOM 276 O LEU A 73 9.771 78.597 14.749 1.00 27.36 A O ATOM 277 N LEU A 74 8.933 77.343 16.401 1.00 27.96 A N ATOM 278 CA LEU A 74 9.321 76.098 15.762 1.00 22.54 A C ATOM 279 CB LEU A 74 9.126 74.931 16.724 1.00 25.45 A C ATOM 280 CG LEU A 74 9.242 73.492 16.222 1.00 21.94 A C ATOM 281 CD1 LEU A 74 9.418 72.592 17.425 1.00 27.44 A C ATOM 282 CD2 LEU A 74 7.998 73.082 15.437 1.00 27.42 A C ATOM 283 C LEU A 74 8.532 75.897 14.474 1.00 25.51 A C ATOM 284 O LEU A 74 9.113 75.559 13.441 1.00 23.54 A O ATOM 285 N GLN A 75 7.217 76.117 14.535 1.00 25.11 A N ATOM 286 CA GLN A 75 6.342 75.965 13.372 1.00 23.19 A C ATOM 287 CB GLN A 75 4.883 76.232 13.756 1.00 23.73 A C ATOM 288 CG GLN A 75 4.264 75.077 14.536 1.00 29.44 A C ATOM 289 CD GLN A 75 3.127 75.504 15.456 1.00 26.10 A C ATOM 290 OE1 GLN A 75 2.794 76.683 15.552 1.00 26.71 A O ATOM 291 NE2 GLN A 75 2.513 74.534 16.115 1.00 21.02 A N ATOM 292 C GLN A 75 6.762 76.895 12.238 1.00 27.74 A C ATOM 293 O GLN A 75 6.651 76.555 11.061 1.00 24.99 A O ATOM 294 N LYS A 76 7.237 78.071 12.613 1.00 23.48 A N ATOM 295 CA LYS A 76 7.755 79.040 11.665 1.00 27.81 A C ATOM 296 CB LYS A 76 7.950 80.384 12.364 1.00 25.62 A C ATOM 297 CG LYS A 76 7.953 81.579 11.436 1.00 40.17 A C ATOM 298 CD LYS A 76 7.964 82.875 12.237 1.00 44.17 A C ATOM 299 CE LYS A 76 6.947 82.836 13.381 1.00 42.30 A C ATOM 300 NZ LYS A 76 5.519 82.808 12.921 1.00 40.55 A N ATOM 301 C LYS A 76 9.082 78.529 11.103 1.00 28.69 A C ATOM 302 O LYS A 76 9.265 78.450 9.885 1.00 23.58 A O ATOM 303 N GLN A 77 9.989 78.153 11.999 1.00 24.27 A N ATOM 304 CA GLN A 77 11.310 77.653 11.598 1.00 25.73 A C ATOM 305 CB GLN A 77 12.196 77.389 12.826 1.00 22.10 A C ATOM 306 CG GLN A 77 13.624 76.905 12.500 1.00 23.74 A C ATOM 307 CD GLN A 77 14.475 77.998 11.878 1.00 29.08 A C ATOM 308 OE1 GLN A 77 14.185 79.180 12.044 1.00 31.00 A O ATOM 309 NE2 GLN A 77 15.531 77.607 11.154 1.00 29.46 A N ATOM 310 C GLN A 77 11.260 76.416 10.704 1.00 21.82 A C ATOM 311 O GLN A 77 12.100 76.264 9.813 1.00 27.38 A O ATOM 312 N LEU A 78 10.271 75.547 10.919 1.00 20.18 A N ATOM 313 CA LEU A 78 10.136 74.299 10.161 1.00 21.85 A C ATOM 314 CB LEU A 78 9.817 73.129 11.088 1.00 19.16 A C ATOM 315 CG LEU A 78 10.877 72.756 12.125 1.00 21.84 A C ATOM 316 CD1 LEU A 78 10.281 71.843 13.192 1.00 22.17 A C ATOM 317 CD2 LEU A 78 12.033 72.084 11.438 1.00 20.71 A C ATOM 318 C LEU A 78 9.076 74.326 9.061 1.00 23.71 A C ATOM 319 O LEU A 78 8.832 73.311 8.410 1.00 24.84 A O ATOM 320 N SER A 79 8.429 75.473 8.882 1.00 28.66 A N ATOM 321 CA SER A 79 7.352 75.637 7.897 1.00 26.88 A C ATOM 322 CB SER A 79 7.887 75.551 6.465 1.00 25.58 A C ATOM 323 OG SER A 79 8.801 76.605 6.225 1.00 30.77 A O ATOM 324 C SER A 79 6.140 74.718 8.074 1.00 25.97 A C ATOM 325 O SER A 79 5.649 74.127 7.111 1.00 24.96 A O ATOM 326 N LEU A 80 5.654 74.622 9.308 1.00 26.48 A N ATOM 327 CA LEU A 80 4.383 73.981 9.600 1.00 23.40 A C ATOM 328 CB LEU A 80 4.528 73.111 10.847 1.00 29.53 A C ATOM 329 CG LEU A 80 5.787 72.252 10.937 1.00 30.61 A C ATOM 330 CD1 LEU A 80 5.914 71.644 12.329 1.00 26.91 A C ATOM 331 CD2 LEU A 80 5.732 71.171 9.879 1.00 28.75 A C ATOM 332 C LEU A 80 3.385 75.092 9.892 1.00 27.46 A C ATOM 333 O LEU A 80 3.790 76.221 10.158 1.00 28.99 A O ATOM 334 N PRO A 81 2.077 74.777 9.896 1.00 30.34 A N ATOM 335 CD PRO A 81 1.427 73.466 9.732 1.00 29.21 A C ATOM 336 CA PRO A 81 1.102 75.836 10.194 1.00 26.61 A C ATOM 337 CB PRO A 81 −0.235 75.081 10.231 1.00 29.96 A C ATOM 338 CG PRO A 81 0.011 73.840 9.419 1.00 29.47 A C ATOM 339 C PRO A 81 1.387 76.491 11.549 1.00 26.37 A C ATOM 340 O PRO A 81 1.567 75.797 12.552 1.00 28.00 A O ATOM 341 N GLU A 82 1.460 77.816 11.564 1.00 29.90 A N ATOM 342 CA GLU A 82 1.761 78.543 12.791 1.00 28.90 A C ATOM 343 CB GLU A 82 2.394 79.895 12.454 1.00 30.37 A C ATOM 344 CG GLU A 82 3.764 79.707 11.786 1.00 30.26 A C ATOM 345 CD GLU A 82 4.040 80.715 10.698 1.00 37.75 A C ATOM 346 OE1 GLU A 82 3.758 81.910 10.929 1.00 37.32 A O ATOM 347 OE2 GLU A 82 4.549 80.313 9.619 1.00 35.51 A O ATOM 348 C GLU A 82 0.507 78.642 13.666 1.00 27.68 A C ATOM 349 O GLU A 82 −0.243 79.613 13.615 1.00 33.78 A O ATOM 350 N THR A 83 0.280 77.588 14.445 1.00 28.57 A N ATOM 351 CA THR A 83 −0.920 77.465 15.255 1.00 29.86 A C ATOM 352 CB THR A 83 −1.521 76.052 15.160 1.00 27.90 A C ATOM 353 OG1 THR A 83 −0.664 75.119 15.839 1.00 28.17 A O ATOM 354 CG2 THR A 83 −1.686 75.628 13.700 1.00 22.38 A C ATOM 355 C THR A 83 −0.595 77.732 16.717 1.00 32.70 A C ATOM 356 O THR A 83 −1.491 77.968 17.519 1.00 26.87 A O ATOM 357 N GLY A 84 0.689 77.690 17.060 1.00 30.42 A N ATOM 358 CA GLY A 84 1.110 77.918 18.433 1.00 27.94 A C ATOM 359 C GLY A 84 0.631 76.843 19.393 1.00 25.62 A C ATOM 360 O GLY A 84 0.670 77.018 20.617 1.00 22.97 A O ATOM 361 N GLU A 85 0.183 75.723 18.840 1.00 23.69 A N ATOM 362 CA GLU A 85 −0.402 74.651 19.640 1.00 27.78 A C ATOM 363 CB GLU A 85 −1.841 74.374 19.171 1.00 27.91 A C ATOM 364 CG GLU A 85 −2.822 75.518 19.398 1.00 22.36 A C ATOM 365 CD GLU A 85 −3.233 75.628 20.864 1.00 27.57 A C ATOM 366 OE1 GLU A 85 −2.995 74.656 21.617 1.00 25.47 A O ATOM 367 OE2 GLU A 85 −3.802 76.674 21.260 1.00 24.16 A O ATOM 368 C GLU A 85 0.410 73.385 19.478 1.00 27.48 A C ATOM 369 O GLU A 85 0.862 73.092 18.382 1.00 28.76 A O ATOM 370 N LEU A 86 0.600 72.630 20.558 1.00 24.11 A N ATOM 371 CA LEU A 86 1.129 71.287 20.418 1.00 24.45 A C ATOM 372 CB LEU A 86 1.515 70.691 21.768 1.00 25.59 A C ATOM 373 CG LEU A 86 2.261 69.348 21.801 1.00 22.97 A C ATOM 374 CD1 LEU A 86 3.599 69.366 21.040 1.00 22.83 A C ATOM 375 CD2 LEU A 86 2.491 68.925 23.235 1.00 27.52 A C ATOM 376 C LEU A 86 0.072 70.450 19.704 1.00 26.07 A C ATOM 377 O LEU A 86 −0.600 69.619 20.309 1.00 28.12 A O ATOM 378 N ASP A 87 −0.064 70.673 18.399 1.00 25.93 A N ATOM 379 CA ASP A 87 −1.026 69.927 17.596 1.00 24.07 A C ATOM 380 CB ASP A 87 −1.690 70.835 16.556 1.00 26.04 A C ATOM 381 CG ASP A 87 −0.683 71.526 15.638 1.00 26.21 A C ATOM 382 OD1 ASP A 87 0.404 70.954 15.379 1.00 26.36 A O ATOM 383 OD2 ASP A 87 −0.995 72.639 15.157 1.00 23.51 A O ATOM 384 C ASP A 87 −0.373 68.722 16.929 1.00 28.57 A C ATOM 385 O ASP A 87 0.806 68.441 17.155 1.00 22.71 A O ATOM 386 N SER A 88 −1.155 68.021 16.111 1.00 34.59 A N ATOM 387 CA SER A 88 −0.740 66.749 15.519 1.00 28.50 A C ATOM 388 CB SER A 88 −1.915 66.071 14.793 1.00 32.79 A C ATOM 389 OG SER A 88 −2.824 65.447 15.702 1.00 33.96 A O ATOM 390 C SER A 88 0.437 66.915 14.562 1.00 27.18 A C ATOM 391 O SER A 88 1.353 66.094 14.559 1.00 29.01 A O ATOM 392 N ALA A 89 0.402 67.962 13.749 1.00 23.17 A N ATOM 393 CA ALA A 89 1.488 68.217 12.817 1.00 28.25 A C ATOM 394 CB ALA A 89 1.186 69.420 11.920 1.00 21.62 A C ATOM 395 C ALA A 89 2.767 68.441 13.600 1.00 28.75 A C ATOM 396 O ALA A 89 3.809 67.892 13.258 1.00 23.14 A O ATOM 397 N THR A 90 2.686 69.234 14.664 1.00 23.35 A N ATOM 398 CA THR A 90 3.880 69.571 15.429 1.00 20.82 A C ATOM 399 CB THR A 90 3.626 70.741 16.392 1.00 19.14 A C ATOM 400 OG1 THR A 90 3.176 71.869 15.637 1.00 23.92 A O ATOM 401 CG2 THR A 90 4.907 71.113 17.119 1.00 25.30 A C ATOM 402 C THR A 90 4.430 68.368 16.164 1.00 21.65 A C ATOM 403 O THR A 90 5.641 68.189 16.282 1.00 22.36 A O ATOM 404 N LEU A 91 3.540 67.517 16.649 1.00 22.58 A N ATOM 405 CA LEU A 91 3.973 66.313 17.334 1.00 19.93 A C ATOM 406 CB LEU A 91 2.772 65.631 17.974 1.00 25.21 A C ATOM 407 CG LEU A 91 3.086 64.714 19.145 1.00 26.78 A C ATOM 408 CD1 LEU A 91 4.108 65.380 20.059 1.00 28.04 A C ATOM 409 CD2 LEU A 91 1.804 64.336 19.901 1.00 27.37 A C ATOM 410 C LEU A 91 4.653 65.367 16.351 1.00 25.26 A C ATOM 411 O LEU A 91 5.725 64.808 16.623 1.00 25.97 A O ATOM 412 N LYS A 92 4.034 65.186 15.197 1.00 28.01 A N ATOM 413 CA LYS A 92 4.626 64.321 14.197 1.00 28.92 A C ATOM 414 CB LYS A 92 3.739 64.224 12.963 1.00 25.40 A C ATOM 415 CG LYS A 92 4.396 63.504 11.809 1.00 32.03 A C ATOM 416 CD LYS A 92 3.534 63.572 10.555 1.00 41.71 A C ATOM 417 CE LYS A 92 4.261 62.992 9.348 1.00 36.44 A C ATOM 418 NZ LYS A 92 3.447 63.149 8.118 1.00 46.89 A N ATOM 419 C LYS A 92 5.995 64.874 13.829 1.00 26.09 A C ATOM 420 O LYS A 92 6.960 64.122 13.711 1.00 26.22 A O ATOM 421 N ALA A 93 6.071 66.187 13.641 1.00 22.82 A N ATOM 422 CA ALA A 93 7.339 66.822 13.303 1.00 24.35 A C ATOM 423 CB ALA A 93 7.162 68.323 13.117 1.00 22.54 A C ATOM 424 C ALA A 93 8.397 66.536 14.367 1.00 23.91 A C ATOM 425 O ALA A 93 9.517 66.131 14.049 1.00 21.21 A O ATOM 426 N MET A 94 8.048 66.765 15.627 1.00 21.87 A N ATOM 427 CA MET A 94 8.961 66.475 16.725 1.00 24.00 A C ATOM 428 CB MET A 94 8.326 66.828 18.064 1.00 24.43 A C ATOM 429 CG MET A 94 8.464 68.288 18.431 1.00 26.48 A C ATOM 430 SD MET A 94 7.149 68.800 19.538 1.00 27.58 A S ATOM 431 CE MET A 94 7.516 70.533 19.810 1.00 23.38 A C ATOM 432 C MET A 94 9.442 65.023 16.760 1.00 26.34 A C ATOM 433 O MET A 94 10.568 64.763 17.189 1.00 23.15 A O ATOM 434 N ARG A 95 8.587 64.085 16.344 1.00 22.91 A N ATOM 435 CA ARG A 95 8.961 62.670 16.306 1.00 25.19 A C ATOM 436 CB ARG A 95 7.724 61.773 16.257 1.00 31.12 A C ATOM 437 CG ARG A 95 6.903 61.732 17.537 1.00 31.41 A C ATOM 438 CD ARG A 95 5.955 60.542 17.487 1.00 35.25 A C ATOM 439 NE ARG A 95 4.930 60.586 18.522 1.00 39.54 A N ATOM 440 CZ ARG A 95 3.678 60.979 18.306 1.00 40.06 A C ATOM 441 NH1 ARG A 95 3.309 61.371 17.088 1.00 36.14 A N ATOM 442 NH2 ARG A 95 2.800 60.982 19.304 1.00 40.43 A N ATOM 443 C ARG A 95 9.876 62.272 15.143 1.00 23.08 A C ATOM 444 O ARG A 95 10.451 61.189 15.153 1.00 28.13 A O ATOM 445 N THR A 96 10.000 63.123 14.137 1.00 23.62 A N ATOM 446 CA THR A 96 10.764 62.759 12.950 1.00 24.74 A C ATOM 447 CB THR A 96 10.371 63.653 11.763 1.00 21.66 A C ATOM 448 OG1 THR A 96 8.945 63.611 11.610 1.00 21.51 A O ATOM 449 CG2 THR A 96 11.021 63.166 10.483 1.00 21.81 A C ATOM 450 C THR A 96 12.278 62.807 13.196 1.00 22.45 A C ATOM 451 O THR A 96 12.785 63.733 13.816 1.00 21.54 A O ATOM 452 N PRO A 97 12.991 61.774 12.738 1.00 17.96 A N ATOM 453 CD PRO A 97 12.376 60.507 12.300 1.00 20.54 A C ATOM 454 CA PRO A 97 14.456 61.697 12.801 1.00 19.25 A C ATOM 455 CB PRO A 97 14.760 60.380 12.081 1.00 22.39 A C ATOM 456 CG PRO A 97 13.519 59.542 12.323 1.00 28.44 A C ATOM 457 C PRO A 97 15.107 62.880 12.082 1.00 15.76 A C ATOM 458 O PRO A 97 14.641 63.315 11.035 1.00 18.84 A O ATOM 459 N ARG A 98 16.168 63.429 12.648 1.00 17.73 A N ATOM 460 CA ARG A 98 16.698 64.682 12.131 1.00 15.49 A C ATOM 461 CB ARG A 98 15.841 65.851 12.601 1.00 12.82 A C ATOM 462 CG ARG A 98 15.782 65.902 14.167 1.00 19.50 A C ATOM 463 CD ARG A 98 15.436 67.283 14.674 1.00 18.83 A C ATOM 464 NE ARG A 98 16.535 68.221 14.453 1.00 18.64 A N ATOM 465 CZ ARG A 98 16.374 69.529 14.298 1.00 19.76 A C ATOM 466 NH1 ARG A 98 15.157 70.046 14.330 1.00 17.16 A N ATOM 467 NH2 ARG A 98 17.427 70.314 14.113 1.00 13.23 A N ATOM 468 C ARG A 98 18.102 64.935 12.624 1.00 17.30 A C ATOM 469 O ARG A 98 18.639 64.166 13.406 1.00 16.57 A O ATOM 470 N CYS A 99 18.665 66.043 12.151 1.00 14.78 A N ATOM 471 CA CYS A 99 19.983 66.523 12.550 1.00 18.24 A C ATOM 472 CB CYS A 99 20.435 67.603 11.565 1.00 17.84 A C ATOM 473 SG CYS A 99 22.057 68.259 11.917 1.00 17.65 A S ATOM 474 C CYS A 99 20.034 67.083 13.976 1.00 20.82 A C ATOM 475 O CYS A 99 19.140 67.801 14.413 1.00 19.67 A O ATOM 476 N GLY A 100 21.101 66.761 14.697 1.00 17.62 A N ATOM 477 CA GLY A 100 21.229 67.208 16.061 1.00 21.71 A C ATOM 478 C GLY A 100 21.768 68.620 16.173 1.00 23.33 A C ATOM 479 O GLY A 100 21.884 69.144 17.274 1.00 19.10 A O ATOM 480 N VAL A 101 22.095 69.249 15.049 1.00 21.53 A N ATOM 481 CA VAL A 101 22.501 70.656 15.120 1.00 20.35 A C ATOM 482 CB VAL A 101 23.186 71.150 13.802 1.00 19.16 A C ATOM 483 CG1 VAL A 101 23.367 72.678 13.807 1.00 24.25 A C ATOM 484 CG2 VAL A 101 24.518 70.500 13.650 1.00 19.32 A C ATOM 485 C VAL A 101 21.282 71.498 15.492 1.00 22.25 A C ATOM 486 O VAL A 101 20.188 71.295 14.962 1.00 20.99 A O ATOM 487 N PRO A 102 21.448 72.424 16.444 1.00 19.27 A N ATOM 488 CD PRO A 102 22.645 72.646 17.271 1.00 22.08 A C ATOM 489 CA PRO A 102 20.342 73.315 16.812 1.00 21.40 A C ATOM 490 CB PRO A 102 20.983 74.258 17.836 1.00 25.88 A C ATOM 491 CG PRO A 102 22.114 73.459 18.421 1.00 28.33 A C ATOM 492 C PRO A 102 19.800 74.124 15.637 1.00 19.41 A C ATOM 493 O PRO A 102 20.509 74.405 14.675 1.00 23.26 A O ATOM 494 N ASP A 103 18.541 74.518 15.741 1.00 20.14 A N ATOM 495 CA ASP A 103 17.871 75.290 14.706 1.00 17.24 A C ATOM 496 CB ASP A 103 16.384 74.973 14.717 1.00 16.86 A C ATOM 497 CG ASP A 103 16.081 73.599 14.206 1.00 15.29 A C ATOM 498 OD1 ASP A 103 16.976 72.968 13.597 1.00 19.58 A O ATOM 499 OD2 ASP A 103 14.932 73.156 14.390 1.00 20.17 A O ATOM 500 C ASP A 103 18.037 76.790 14.895 1.00 22.99 A C ATOM 501 O ASP A 103 18.147 77.541 13.922 1.00 20.29 A O ATOM 502 N LEU A 104 18.005 77.226 16.149 1.00 21.05 A N ATOM 503 CA LEU A 104 18.171 78.636 16.491 1.00 25.44 A C ATOM 504 CB LEU A 104 16.881 79.187 17.106 1.00 25.74 A C ATOM 505 CG LEU A 104 15.710 79.464 16.156 1.00 22.13 A C ATOM 506 CD1 LEU A 104 14.425 79.771 16.925 1.00 26.55 A C ATOM 507 CD2 LEU A 104 16.046 80.642 15.253 1.00 21.34 A C ATOM 508 C LEU A 104 19.316 78.710 17.487 1.00 29.77 A C ATOM 509 O LEU A 104 19.272 78.068 18.525 1.00 32.01 A O ATOM 510 N GLY A 105 20.351 79.482 17.181 1.00 36.14 A N ATOM 511 CA GLY A 105 21.592 79.355 17.927 1.00 39.27 A C ATOM 512 C GLY A 105 22.438 78.298 17.241 1.00 39.73 A C ATOM 513 O GLY A 105 22.106 77.951 16.108 1.00 41.34 A O ATOM 514 N ARG A 106 23.512 77.763 17.833 1.00 43.54 A N ATOM 515 CA ARG A 106 24.089 78.038 19.155 1.00 44.07 A C ATOM 516 CB ARG A 106 23.253 78.977 20.034 1.00 42.88 A C ATOM 517 CG ARG A 106 23.802 80.424 20.166 1.00 41.91 A C ATOM 518 CD ARG A 106 23.829 81.167 18.821 1.00 44.85 A C ATOM 519 NE ARG A 106 23.718 82.622 18.950 1.00 42.04 A N ATOM 520 CZ ARG A 106 23.550 83.452 17.923 1.00 36.44 A C ATOM 521 NH1 ARG A 106 23.459 84.757 18.124 1.00 38.36 A N ATOM 522 NH2 ARG A 106 23.469 82.979 16.692 1.00 41.73 A N ATOM 523 C ARG A 106 24.391 76.713 19.875 1.00 39.64 A C ATOM 524 O ARG A 106 23.813 76.423 20.925 1.00 35.55 A O ATOM 525 N PHE A 107 25.274 75.901 19.286 1.00 35.00 A N ATOM 526 CA PHE A 107 25.849 74.755 19.989 1.00 34.23 A C ATOM 527 CB PHE A 107 26.867 74.040 19.106 1.00 34.59 A C ATOM 528 CG PHE A 107 26.439 72.668 18.648 1.00 30.45 A C ATOM 529 CD1 PHE A 107 25.581 71.894 19.414 1.00 29.91 A C ATOM 530 CD2 PHE A 107 26.940 72.142 17.466 1.00 24.85 A C ATOM 531 CE1 PHE A 107 25.197 70.625 18.983 1.00 35.05 A C ATOM 532 CE2 PHE A 107 26.580 70.878 17.034 1.00 21.61 A C ATOM 533 CZ PHE A 107 25.711 70.116 17.783 1.00 28.46 A C ATOM 534 C PHE A 107 26.588 75.291 21.207 1.00 40.86 A C ATOM 535 O PHE A 107 26.453 74.793 22.338 1.00 41.15 A O ATOM 536 N GLN A 108 27.387 76.317 20.937 1.00 36.20 A N ATOM 537 CA GLN A 108 28.185 77.007 21.925 1.00 36.81 A C ATOM 538 CB GLN A 108 29.350 76.121 22.371 1.00 35.59 A C ATOM 539 CG GLN A 108 30.246 75.678 21.241 1.00 33.01 A C ATOM 540 CD GLN A 108 31.218 74.577 21.660 1.00 44.05 A C ATOM 541 OE1 GLN A 108 30.809 73.474 22.038 1.00 39.08 A O ATOM 542 NE2 GLN A 108 32.515 74.869 21.580 1.00 42.04 A N ATOM 543 C GLN A 108 28.677 78.229 21.172 1.00 36.68 A C ATOM 544 O GLN A 108 28.313 78.414 20.007 1.00 33.95 A O ATOM 545 N THR A 109 29.468 79.086 21.805 1.00 36.38 A N ATOM 546 CA THR A 109 30.136 80.112 21.024 1.00 30.02 A C ATOM 547 CB THR A 109 30.514 81.344 21.852 1.00 36.60 A C ATOM 548 OG1 THR A 109 31.385 80.958 22.920 1.00 38.46 A O ATOM 549 CG2 THR A 109 29.272 81.975 22.416 1.00 24.66 A C ATOM 550 C THR A 109 31.366 79.484 20.400 1.00 35.20 A C ATOM 551 O THR A 109 32.056 78.678 21.037 1.00 35.53 A O ATOM 552 N PHE A 110 31.613 79.827 19.141 1.00 30.25 A N ATOM 553 CA PHE A 110 32.679 79.210 18.369 1.00 30.77 A C ATOM 554 CB PHE A 110 32.108 78.592 17.091 1.00 25.57 A C ATOM 555 CG PHE A 110 31.391 77.289 17.313 1.00 29.18 A C ATOM 556 CD1 PHE A 110 30.023 77.188 17.120 1.00 25.98 A C ATOM 557 CD2 PHE A 110 32.090 76.164 17.710 1.00 24.26 A C ATOM 558 CE1 PHE A 110 29.374 75.988 17.301 1.00 26.02 A C ATOM 559 CE2 PHE A 110 31.443 74.961 17.901 1.00 26.73 A C ATOM 560 CZ PHE A 110 30.083 74.872 17.700 1.00 28.94 A C ATOM 561 C PHE A 110 33.748 80.231 18.010 1.00 30.51 A C ATOM 562 O PHE A 110 33.516 81.435 18.102 1.00 29.17 A O ATOM 563 N GLU A 111 34.913 79.744 17.595 1.00 29.42 A N ATOM 564 CA GLU A 111 35.996 80.609 17.170 1.00 28.87 A C ATOM 565 CB GLU A 111 37.347 79.931 17.387 1.00 29.93 A C ATOM 566 CG GLU A 111 37.750 79.731 18.835 1.00 39.56 A C ATOM 567 CD GLU A 111 39.236 79.414 18.972 1.00 43.87 A C ATOM 568 OE1 GLU A 111 40.009 79.790 18.064 1.00 53.02 A O ATOM 569 OE2 GLU A 111 39.635 78.802 19.983 1.00 45.00 A O ATOM 570 C GLU A 111 35.878 80.994 15.704 1.00 34.76 A C ATOM 571 O GLU A 111 35.593 80.152 14.845 1.00 32.30 A O ATOM 572 N GLY A 112 36.120 82.272 15.425 1.00 30.28 A N ATOM 573 CA GLY A 112 36.220 82.759 14.061 1.00 33.11 A C ATOM 574 C GLY A 112 34.901 83.226 13.485 1.00 28.91 A C ATOM 575 O GLY A 112 33.892 83.273 14.189 1.00 28.66 A O ATOM 576 N ASP A 113 34.917 83.569 12.202 1.00 27.21 A N ATOM 577 CA ASP A 113 33.716 83.982 11.476 1.00 28.09 A C ATOM 578 CB ASP A 113 34.094 85.017 10.418 1.00 29.22 A C ATOM 579 CG ASP A 113 34.862 84.410 9.253 1.00 27.67 A C ATOM 580 OD1 ASP A 113 35.125 83.193 9.263 1.00 32.88 A O ATOM 581 OD2 ASP A 113 35.201 85.157 8.322 1.00 29.35 A O ATOM 582 C ASP A 113 32.926 82.825 10.820 1.00 25.49 A C ATOM 583 O ASP A 113 31.950 83.061 10.111 1.00 25.86 A O ATOM 584 N LEU A 114 33.388 81.595 11.024 1.00 23.45 A N ATOM 585 CA LEU A 114 32.653 80.373 10.640 1.00 28.12 A C ATOM 586 CB LEU A 114 31.266 80.336 11.276 1.00 23.09 A C ATOM 587 CG LEU A 114 31.208 80.655 12.770 1.00 31.83 A C ATOM 588 CD1 LEU A 114 29.760 80.725 13.206 1.00 26.63 A C ATOM 589 CD2 LEU A 114 31.979 79.623 13.603 1.00 28.05 A C ATOM 590 C LEU A 114 32.526 80.089 9.148 1.00 28.25 A C ATOM 591 O LEU A 114 31.556 79.454 8.699 1.00 23.52 A O ATOM 592 N LYS A 115 33.504 80.545 8.379 1.00 26.54 A N ATOM 593 CA LYS A 115 33.674 80.049 7.024 1.00 27.29 A C ATOM 594 CB LYS A 115 33.165 81.056 5.986 1.00 30.13 A C ATOM 595 CG LYS A 115 34.153 82.148 5.596 1.00 28.06 A C ATOM 596 CD LYS A 115 33.579 82.997 4.462 1.00 33.60 A C ATOM 597 CE LYS A 115 34.669 83.734 3.712 1.00 31.03 A C ATOM 598 NZ LYS A 115 34.111 84.528 2.581 1.00 44.10 A N ATOM 599 C LYS A 115 35.146 79.749 6.851 1.00 23.25 A C ATOM 600 O LYS A 115 35.967 80.286 7.580 1.00 27.93 A O ATOM 601 N TRP A 116 35.476 78.871 5.913 1.00 21.61 A N ATOM 602 CA TRP A 116 36.874 78.514 5.643 1.00 28.50 A C ATOM 603 CB TRP A 116 36.952 77.241 4.794 1.00 23.28 A C ATOM 604 CG TRP A 116 36.449 76.035 5.495 1.00 24.16 A C ATOM 605 CD2 TRP A 116 37.053 75.392 6.617 1.00 21.27 A C ATOM 606 CE2 TRP A 116 36.248 74.292 6.952 1.00 21.43 A C ATOM 607 CE3 TRP A 116 38.190 75.656 7.385 1.00 23.79 A C ATOM 608 CD1 TRP A 116 35.332 75.315 5.196 1.00 19.51 A C ATOM 609 NE1 TRP A 116 35.201 74.266 6.069 1.00 18.49 A N ATOM 610 CZ2 TRP A 116 36.544 73.445 8.019 1.00 23.72 A C ATOM 611 CZ3 TRP A 116 38.490 74.802 8.444 1.00 27.02 A C ATOM 612 CH2 TRP A 116 37.665 73.716 8.749 1.00 23.04 A C ATOM 613 C TRP A 116 37.596 79.626 4.901 1.00 30.80 A C ATOM 614 O TRP A 116 37.009 80.275 4.029 1.00 28.73 A O ATOM 615 N HIS A 117 38.876 79.818 5.215 1.00 28.53 A N ATOM 616 CA HIS A 117 39.682 80.804 4.500 1.00 32.77 A C ATOM 617 CB HIS A 117 40.125 81.925 5.449 1.00 29.30 A C ATOM 618 CG HIS A 117 38.989 82.738 5.976 1.00 30.21 A C ATOM 619 CD2 HIS A 117 38.261 83.725 5.405 1.00 30.22 A C ATOM 620 ND1 HIS A 117 38.460 82.550 7.235 1.00 36.49 A N ATOM 621 CE1 HIS A 117 37.462 83.394 7.422 1.00 31.51 A C ATOM 622 NE2 HIS A 117 37.320 84.118 6.326 1.00 32.15 A N ATOM 623 C HIS A 117 40.860 80.191 3.718 1.00 30.79 A C ATOM 624 O HIS A 117 41.897 80.833 3.505 1.00 27.54 A O ATOM 625 N HIS A 118 40.679 78.940 3.309 1.00 21.23 A N ATOM 626 CA HIS A 118 41.492 78.315 2.281 1.00 25.23 A C ATOM 627 CB HIS A 118 42.600 77.427 2.851 1.00 23.56 A C ATOM 628 CG HIS A 118 42.113 76.357 3.778 1.00 20.78 A C ATOM 629 CD2 HIS A 118 42.084 75.009 3.652 1.00 22.92 A C ATOM 630 ND1 HIS A 118 41.622 76.635 5.036 1.00 25.15 A N ATOM 631 CE1 HIS A 118 41.284 75.504 5.633 1.00 26.08 A C ATOM 632 NE2 HIS A 118 41.559 74.502 4.818 1.00 20.92 A N ATOM 633 C HIS A 118 40.559 77.509 1.396 1.00 24.66 A C ATOM 634 O HIS A 118 39.361 77.428 1.661 1.00 28.91 A O ATOM 635 N HIS A 119 41.134 76.885 0.378 1.00 27.88 A N ATOM 636 CA HIS A 119 40.392 76.358 −0.750 1.00 27.48 A C ATOM 637 CB HIS A 119 41.043 76.887 −2.038 1.00 30.54 A C ATOM 638 CG HIS A 119 40.661 76.152 −3.285 1.00 36.56 A C ATOM 639 CD2 HIS A 119 41.226 75.086 −3.905 1.00 38.04 A C ATOM 640 ND1 HIS A 119 39.610 76.544 −4.090 1.00 41.04 A N ATOM 641 CE1 HIS A 119 39.522 75.731 −5.128 1.00 34.65 A C ATOM 642 NE2 HIS A 119 40.492 74.837 −5.041 1.00 34.66 A N ATOM 643 C HIS A 119 40.361 74.848 −0.730 1.00 27.23 A C ATOM 644 O HIS A 119 39.333 74.240 −1.031 1.00 31.66 A O ATOM 645 N ASN A 120 41.487 74.232 −0.399 1.00 21.91 A N ATOM 646 CA ASN A 120 41.519 72.792 −0.342 1.00 25.25 A C ATOM 647 CB ASN A 120 42.858 72.233 −0.814 1.00 28.33 A C ATOM 648 CG ASN A 120 42.839 70.722 −0.921 1.00 34.17 A C ATOM 649 OD1 ASN A 120 41.774 70.095 −0.887 1.00 31.52 A O ATOM 650 ND2 ASN A 120 44.021 70.121 −1.026 1.00 33.79 A N ATOM 651 C ASN A 120 41.203 72.312 1.066 1.00 25.06 A C ATOM 652 O ASN A 120 42.040 72.378 1.965 1.00 29.38 A O ATOM 653 N ILE A 121 39.980 71.837 1.245 1.00 26.62 A N ATOM 654 CA ILE A 121 39.536 71.330 2.530 1.00 22.88 A C ATOM 655 CB ILE A 121 38.016 71.479 2.675 1.00 23.40 A C ATOM 656 CG2 ILE A 121 37.577 71.230 4.120 1.00 19.11 A C ATOM 657 CG1 ILE A 121 37.597 72.885 2.228 1.00 25.97 A C ATOM 658 CD1 ILE A 121 38.220 73.994 3.050 1.00 24.47 A C ATOM 659 C ILE A 121 39.939 69.878 2.606 1.00 22.59 A C ATOM 660 O ILE A 121 39.642 69.089 1.707 1.00 24.78 A O ATOM 661 N THR A 122 40.643 69.514 3.667 1.00 23.63 A N ATOM 662 CA THR A 122 41.092 68.142 3.800 1.00 21.19 A C ATOM 663 CB THR A 122 42.549 68.078 4.267 1.00 17.91 A C ATOM 664 OG1 THR A 122 42.669 68.769 5.514 1.00 25.42 A O ATOM 665 CG2 THR A 122 43.440 68.775 3.248 1.00 23.17 A C ATOM 666 C THR A 122 40.177 67.478 4.804 1.00 22.00 A C ATOM 667 O THR A 122 39.612 68.141 5.664 1.00 23.82 A O ATOM 668 N TYR A 123 39.980 66.176 4.671 1.00 24.37 A N ATOM 669 CA TYR A 123 39.085 65.491 5.584 1.00 22.56 A C ATOM 670 CB TYR A 123 37.672 65.358 5.006 1.00 19.38 A C ATOM 671 CG TYR A 123 37.555 64.439 3.813 1.00 18.63 A C ATOM 672 CD1 TYR A 123 37.655 64.937 2.528 1.00 20.49 A C ATOM 673 CE1 TYR A 123 37.541 64.117 1.424 1.00 22.04 A C ATOM 674 CD2 TYR A 123 37.292 63.079 3.971 1.00 22.95 A C ATOM 675 CE2 TYR A 123 37.161 62.241 2.869 1.00 22.24 A C ATOM 676 CZ TYR A 123 37.292 62.767 1.597 1.00 22.45 A C ATOM 677 OH TYR A 123 37.150 61.963 0.486 1.00 25.84 A O ATOM 678 C TYR A 123 39.642 64.128 5.925 1.00 21.92 A C ATOM 679 O TYR A 123 40.284 63.497 5.107 1.00 21.37 A O ATOM 680 N TRP A 124 39.387 63.693 7.150 1.00 21.82 A N ATOM 681 CA TRP A 124 39.923 62.437 7.632 1.00 23.65 A C ATOM 682 CB TRP A 124 40.901 62.706 8.764 1.00 24.93 A C ATOM 683 CG TRP A 124 41.506 61.467 9.350 1.00 26.30 A C ATOM 684 CD2 TRP A 124 41.930 61.284 10.704 1.00 29.98 A C ATOM 685 CE2 TRP A 124 42.453 59.982 10.806 1.00 30.27 A C ATOM 686 CE3 TRP A 124 41.916 62.094 11.841 1.00 32.92 A C ATOM 687 CD1 TRP A 124 41.789 60.315 8.703 1.00 28.63 A C ATOM 688 NE1 TRP A 124 42.348 59.405 9.571 1.00 27.65 A N ATOM 689 CZ2 TRP A 124 42.962 59.472 11.998 1.00 28.60 A C ATOM 690 CZ3 TRP A 124 42.419 61.588 13.019 1.00 34.96 A C ATOM 691 CH2 TRP A 124 42.928 60.285 13.091 1.00 30.56 A C ATOM 692 C TRP A 124 38.802 61.545 8.116 1.00 19.47 A C ATOM 693 O TRP A 124 38.008 61.944 8.967 1.00 25.79 A O ATOM 694 N ILE A 125 38.721 60.337 7.573 1.00 23.99 A N ATOM 695 CA ILE A 125 37.727 59.384 8.049 1.00 20.20 A C ATOM 696 CB ILE A 125 37.313 58.407 6.942 1.00 26.29 A C ATOM 697 CG2 ILE A 125 36.308 57.415 7.464 1.00 20.06 A C ATOM 698 CG1 ILE A 125 36.704 59.168 5.766 1.00 23.59 A C ATOM 699 CD1 ILE A 125 36.810 58.436 4.463 1.00 24.73 A C ATOM 700 C ILE A 125 38.314 58.627 9.249 1.00 24.20 A C ATOM 701 O ILE A 125 38.996 57.618 9.078 1.00 26.23 A O ATOM 702 N GLN A 126 38.046 59.127 10.455 1.00 27.66 A N ATOM 703 CA GLN A 126 38.759 58.688 11.657 1.00 28.10 A C ATOM 704 CB GLN A 126 38.502 59.638 12.831 1.00 29.85 A C ATOM 705 CG GLN A 126 39.200 59.189 14.113 1.00 32.51 A C ATOM 706 CD GLN A 126 39.023 60.147 15.283 1.00 37.58 A C ATOM 707 OE1 GLN A 126 38.010 60.847 15.406 1.00 36.41 A O ATOM 708 NE2 GLN A 126 40.009 60.160 16.170 1.00 39.88 A N ATOM 709 C GLN A 126 38.436 57.258 12.077 1.00 27.75 A C ATOM 710 O GLN A 126 39.290 56.554 12.610 1.00 31.90 A O ATOM 711 N ASN A 127 37.193 56.849 11.858 1.00 23.85 A N ATOM 712 CA ASN A 127 36.773 55.484 12.117 1.00 22.94 A C ATOM 713 CB ASN A 127 36.465 55.248 13.613 1.00 23.45 A C ATOM 714 CG ASN A 127 35.238 56.007 14.112 1.00 24.46 A C ATOM 715 OD1 ASN A 127 34.630 56.789 13.387 1.00 21.59 A O ATOM 716 ND2 ASN A 127 34.880 55.783 15.379 1.00 21.93 A N ATOM 717 C ASN A 127 35.617 55.130 11.195 1.00 22.01 A C ATOM 718 O ASN A 127 35.219 55.947 10.367 1.00 22.97 A O ATOM 719 N TYR A 128 35.105 53.914 11.313 1.00 22.09 A N ATOM 720 CA TYR A 128 34.068 53.418 10.425 1.00 22.49 A C ATOM 721 CB TYR A 128 34.654 52.387 9.469 1.00 24.51 A C ATOM 722 CG TYR A 128 35.541 52.949 8.380 1.00 27.71 A C ATOM 723 CD1 TYR A 128 35.026 53.224 7.127 1.00 25.18 A C ATOM 724 CE1 TYR A 128 35.824 53.722 6.111 1.00 29.94 A C ATOM 725 CD2 TYR A 128 36.897 53.179 8.600 1.00 26.61 A C ATOM 726 CE2 TYR A 128 37.712 53.691 7.588 1.00 26.46 A C ATOM 727 CZ TYR A 128 37.162 53.956 6.346 1.00 31.21 A C ATOM 728 OH TYR A 128 37.938 54.453 5.332 1.00 22.97 A O ATOM 729 C TYR A 128 32.951 52.733 11.201 1.00 28.11 A C ATOM 730 O TYR A 128 33.210 52.104 12.233 1.00 26.32 A O ATOM 731 N SER A 129 31.720 52.842 10.696 1.00 22.44 A N ATOM 732 CA SER A 129 30.648 51.940 11.108 1.00 21.32 A C ATOM 733 CB SER A 129 29.288 52.521 10.706 1.00 22.95 A C ATOM 734 OG SER A 129 28.258 51.540 10.740 1.00 24.54 A O ATOM 735 C SER A 129 30.839 50.588 10.421 1.00 26.13 A C ATOM 736 O SER A 129 31.322 50.540 9.292 1.00 25.04 A O ATOM 737 N GLU A 130 30.443 49.501 11.090 1.00 23.70 A N ATOM 738 CA GLU A 130 30.492 48.165 10.503 1.00 26.52 A C ATOM 739 CB GLU A 130 30.730 47.102 11.586 1.00 31.69 A C ATOM 740 CG GLU A 130 31.987 47.301 12.406 1.00 28.11 A C ATOM 741 CD GLU A 130 33.237 47.299 11.561 1.00 37.73 A C ATOM 742 OE1 GLU A 130 33.404 46.368 10.738 1.00 35.94 A O ATOM 743 OE2 GLU A 130 34.061 48.222 11.736 1.00 38.46 A O ATOM 744 C GLU A 130 29.202 47.834 9.769 1.00 29.13 A C ATOM 745 O GLU A 130 28.977 46.692 9.370 1.00 26.77 A O ATOM 746 N ASP A 131 28.334 48.826 9.601 1.00 27.87 A N ATOM 747 CA ASP A 131 27.070 48.579 8.918 1.00 24.17 A C ATOM 748 CB ASP A 131 26.066 49.710 9.188 1.00 23.88 A C ATOM 749 CG ASP A 131 25.510 49.667 10.594 1.00 26.68 A C ATOM 750 OD1 ASP A 131 25.543 48.580 11.211 1.00 26.57 A O ATOM 751 OD2 ASP A 131 25.014 50.707 11.084 1.00 26.71 A O ATOM 752 C ASP A 131 27.253 48.360 7.406 1.00 25.89 A C ATOM 753 O ASP A 131 26.508 47.599 6.799 1.00 24.26 A O ATOM 754 N LEU A 132 28.256 49.017 6.823 1.00 24.14 A N ATOM 755 CA LEU A 132 28.532 48.965 5.395 1.00 24.32 A C ATOM 756 CB LEU A 132 28.200 50.314 4.757 1.00 24.53 A C ATOM 757 CG LEU A 132 26.768 50.837 4.865 1.00 29.64 A C ATOM 758 CD1 LEU A 132 26.745 52.368 4.845 1.00 21.15 A C ATOM 759 CD2 LEU A 132 25.924 50.256 3.723 1.00 26.72 A C ATOM 760 C LEU A 132 30.027 48.696 5.195 1.00 25.31 A C ATOM 761 O LEU A 132 30.831 48.980 6.078 1.00 24.25 A O ATOM 762 N PRO A 133 30.408 48.168 4.023 1.00 26.12 A N ATOM 763 CD PRO A 133 29.553 47.651 2.948 1.00 24.69 A C ATOM 764 CA PRO A 133 31.829 47.979 3.719 1.00 26.34 A C ATOM 765 CB PRO A 133 31.808 47.364 2.320 1.00 23.15 A C ATOM 766 CG PRO A 133 30.473 46.729 2.227 1.00 17.02 A C ATOM 767 C PRO A 133 32.540 49.312 3.702 1.00 26.05 A C ATOM 768 O PRO A 133 31.908 50.337 3.447 1.00 22.01 A O ATOM 769 N ARG A 134 33.837 49.300 3.986 1.00 21.09 A N ATOM 770 CA ARG A 134 34.578 50.536 4.127 1.00 25.51 A C ATOM 771 CB ARG A 134 35.943 50.260 4.724 1.00 28.49 A C ATOM 772 CG ARG A 134 35.878 49.879 6.187 1.00 33.05 A C ATOM 773 CD ARG A 134 37.274 49.784 6.784 1.00 36.72 A C ATOM 774 NE ARG A 134 37.235 49.774 8.240 1.00 37.75 A N ATOM 775 CZ ARG A 134 38.288 50.026 9.007 1.00 38.85 A C ATOM 776 NH1 ARG A 134 39.460 50.312 8.444 1.00 40.15 A N ATOM 777 NH2 ARG A 134 38.171 50.005 10.329 1.00 34.77 A N ATOM 778 C ARG A 134 34.719 51.294 2.806 1.00 25.23 A C ATOM 779 O ARG A 134 34.850 52.519 2.795 1.00 24.77 A O ATOM 780 N ALA A 135 34.698 50.569 1.696 1.00 21.16 A N ATOM 781 CA ALA A 135 34.763 51.209 0.387 1.00 22.34 A C ATOM 782 CB ALA A 135 34.998 50.183 −0.688 1.00 28.75 A C ATOM 783 C ALA A 135 33.483 52.002 0.109 1.00 20.44 A C ATOM 784 O ALA A 135 33.517 53.068 −0.490 1.00 25.81 A O ATOM 785 N VAL A 136 32.365 51.481 0.588 1.00 25.86 A N ATOM 786 CA VAL A 136 31.062 52.060 0.329 1.00 26.18 A C ATOM 787 CB VAL A 136 29.950 51.033 0.614 1.00 24.57 A C ATOM 788 CG1 VAL A 136 28.587 51.703 0.699 1.00 26.39 A C ATOM 789 CG2 VAL A 136 29.956 49.965 −0.460 1.00 22.04 A C ATOM 790 C VAL A 136 30.867 53.308 1.165 1.00 22.89 A C ATOM 791 O VAL A 136 30.134 54.212 0.771 1.00 22.68 A O ATOM 792 N ILE A 137 31.552 53.339 2.304 1.00 22.18 A N ATOM 793 CA ILE A 137 31.563 54.472 3.224 1.00 21.81 A C ATOM 794 CB ILE A 137 31.997 54.012 4.635 1.00 23.27 A C ATOM 795 CG2 ILE A 137 32.328 55.220 5.535 1.00 21.30 A C ATOM 796 CG1 ILE A 137 30.935 53.104 5.254 1.00 21.83 A C ATOM 797 CD1 ILE A 137 31.244 52.666 6.674 1.00 27.08 A C ATOM 798 C ILE A 137 32.516 55.558 2.716 1.00 22.09 A C ATOM 799 O ILE A 137 32.184 56.764 2.731 1.00 19.52 A O ATOM 800 N ASP A 138 33.685 55.132 2.241 1.00 15.51 A N ATOM 801 CA ASP A 138 34.601 56.057 1.577 1.00 21.68 A C ATOM 802 CB ASP A 138 35.863 55.343 1.091 1.00 20.32 A C ATOM 803 CG ASP A 138 36.688 54.746 2.231 1.00 27.56 A C ATOM 804 OD1 ASP A 138 36.316 54.934 3.402 1.00 28.65 A O ATOM 805 OD2 ASP A 138 37.711 54.080 1.950 1.00 26.14 A O ATOM 806 C ASP A 138 33.898 56.727 0.400 1.00 19.81 A C ATOM 807 O ASP A 138 33.959 57.949 0.236 1.00 21.48 A O ATOM 808 N ASP A 139 33.211 55.934 −0.409 1.00 18.72 A N ATOM 809 CA ASP A 139 32.572 56.469 −1.603 1.00 23.38 A C ATOM 810 CB ASP A 139 32.219 55.348 −2.578 1.00 23.62 A C ATOM 811 CG ASP A 139 31.236 55.791 −3.651 1.00 23.82 A C ATOM 812 OD1 ASP A 139 31.668 56.378 −4.666 1.00 25.26 A O ATOM 813 OD2 ASP A 139 30.025 55.530 −3.484 1.00 32.34 A O ATOM 814 C ASP A 139 31.335 57.310 −1.280 1.00 19.58 A C ATOM 815 O ASP A 139 31.004 58.260 −2.011 1.00 19.11 A O ATOM 816 N ALA A 140 30.648 56.963 −0.198 1.00 21.49 A N ATOM 817 CA ALA A 140 29.490 57.745 0.237 1.00 17.36 A C ATOM 818 CB ALA A 140 28.784 57.056 1.416 1.00 22.48 A C ATOM 819 C ALA A 140 29.920 59.165 0.616 1.00 19.30 A C ATOM 820 O ALA A 140 29.294 60.155 0.224 1.00 19.66 A O ATOM 821 N PHE A 141 30.995 59.262 1.381 1.00 19.18 A N ATOM 822 CA PHE A 141 31.532 60.558 1.795 1.00 21.07 A C ATOM 823 CB PHE A 141 32.600 60.367 2.884 1.00 19.86 A C ATOM 824 CG PHE A 141 32.040 59.924 4.219 1.00 17.04 A C ATOM 825 CD1 PHE A 141 30.872 60.474 4.714 1.00 20.55 A C ATOM 826 CD2 PHE A 141 32.702 58.985 4.985 1.00 24.18 A C ATOM 827 CE1 PHE A 141 30.359 60.079 5.952 1.00 19.03 A C ATOM 828 CE2 PHE A 141 32.194 58.586 6.219 1.00 21.80 A C ATOM 829 CZ PHE A 141 31.020 59.138 6.691 1.00 13.78 A C ATOM 830 C PHE A 141 32.112 61.351 0.615 1.00 19.94 A C ATOM 831 O PHE A 141 31.947 62.570 0.527 1.00 20.51 A O ATOM 832 N ALA A 142 32.802 60.653 −0.277 1.00 22.37 A N ATOM 833 CA ALA A 142 33.400 61.287 −1.436 1.00 24.59 A C ATOM 834 CB ALA A 142 34.276 60.303 −2.202 1.00 21.91 A C ATOM 835 C ALA A 142 32.301 61.874 −2.322 1.00 21.92 A C ATOM 836 O ALA A 142 32.423 62.998 −2.783 1.00 21.29 A O ATOM 837 N ARG A 143 31.207 61.135 −2.510 1.00 22.50 A N ATOM 838 CA ARG A 143 30.099 61.604 −3.362 1.00 20.60 A C ATOM 839 CB ARG A 143 29.129 60.449 −3.665 1.00 18.06 A C ATOM 840 CG ARG A 143 29.738 59.327 −4.535 1.00 19.78 A C ATOM 841 CD ARG A 143 28.945 58.014 −4.469 1.00 26.88 A C ATOM 842 NE ARG A 143 27.532 58.329 −4.385 1.00 29.07 A N ATOM 843 CZ ARG A 143 26.652 57.801 −3.536 1.00 22.70 A C ATOM 844 NH1 ARG A 143 26.973 56.855 −2.654 1.00 24.34 A N ATOM 845 NH2 ARG A 143 25.409 58.239 −3.593 1.00 20.42 A N ATOM 846 C ARG A 143 29.388 62.787 −2.681 1.00 22.44 A C ATOM 847 O ARG A 143 28.975 63.757 −3.337 1.00 19.75 A O ATOM 848 N ALA A 144 29.287 62.723 −1.356 1.00 20.57 A N ATOM 849 CA ALA A 144 28.703 63.805 −0.580 1.00 18.59 A C ATOM 850 CB ALA A 144 28.615 63.420 0.941 1.00 17.49 A C ATOM 851 C ALA A 144 29.482 65.102 −0.760 1.00 19.82 A C ATOM 852 O ALA A 144 28.890 66.182 −0.895 1.00 18.09 A O ATOM 853 N PHE A 145 30.808 64.994 −0.753 1.00 17.79 A N ATOM 854 CA PHE A 145 31.673 66.151 −0.979 1.00 16.91 A C ATOM 855 CB PHE A 145 33.136 65.837 −0.647 1.00 17.02 A C ATOM 856 CG PHE A 145 33.444 65.824 0.846 1.00 17.43 A C ATOM 857 CD1 PHE A 145 33.142 66.919 1.645 1.00 17.74 A C ATOM 858 CD2 PHE A 145 34.071 64.733 1.429 1.00 16.59 A C ATOM 859 CE1 PHE A 145 33.436 66.909 3.020 1.00 22.03 A C ATOM 860 CE2 PHE A 145 34.375 64.714 2.783 1.00 21.56 A C ATOM 861 CZ PHE A 145 34.061 65.803 3.582 1.00 18.75 A C ATOM 862 C PHE A 145 31.571 66.666 −2.402 1.00 19.26 A C ATOM 863 O PHE A 145 31.534 67.878 −2.619 1.00 16.59 A O ATOM 864 N ALA A 146 31.532 65.746 −3.366 1.00 18.45 A N ATOM 865 CA ALA A 146 31.446 66.129 −4.768 1.00 20.68 A C ATOM 866 CB ALA A 146 31.413 64.900 −5.667 1.00 14.76 A C ATOM 867 C ALA A 146 30.222 67.013 −5.009 1.00 19.39 A C ATOM 868 O ALA A 146 30.253 67.886 −5.851 1.00 21.00 A O ATOM 869 N LEU A 147 29.146 66.785 −4.270 1.00 18.32 A N ATOM 870 CA LEU A 147 28.000 67.679 −4.374 1.00 17.77 A C ATOM 871 CB LEU A 147 26.916 67.309 −3.382 1.00 15.53 A C ATOM 872 CG LEU A 147 26.243 65.948 −3.556 1.00 15.55 A C ATOM 873 CD1 LEU A 147 25.377 65.646 −2.350 1.00 19.53 A C ATOM 874 CD2 LEU A 147 25.400 65.930 −4.859 1.00 16.11 A C ATOM 875 C LEU A 147 28.423 69.129 −4.151 1.00 20.88 A C ATOM 876 O LEU A 147 28.063 70.003 −4.940 1.00 19.37 A O ATOM 877 N TRP A 148 29.163 69.380 −3.067 1.00 18.54 A N ATOM 878 CA TRP A 148 29.527 70.747 −2.691 1.00 17.49 A C ATOM 879 CB TRP A 148 29.852 70.856 −1.183 1.00 18.66 A C ATOM 880 CG TRP A 148 28.655 70.553 −0.315 1.00 15.04 A C ATOM 881 CD2 TRP A 148 27.478 71.355 −0.173 1.00 18.67 A C ATOM 882 CE2 TRP A 148 26.606 70.671 0.710 1.00 16.56 A C ATOM 883 CE3 TRP A 148 27.080 72.592 −0.694 1.00 17.02 A C ATOM 884 CD1 TRP A 148 28.444 69.431 0.446 1.00 17.21 A C ATOM 885 NE1 TRP A 148 27.218 69.500 1.066 1.00 19.54 A N ATOM 886 CZ2 TRP A 148 25.360 71.184 1.083 1.00 21.39 A C ATOM 887 CZ3 TRP A 148 25.843 73.100 −0.324 1.00 17.16 A C ATOM 888 CH2 TRP A 148 24.992 72.389 0.545 1.00 15.76 A C ATOM 889 C TRP A 148 30.646 71.333 −3.554 1.00 19.17 A C ATOM 890 O TRP A 148 30.642 72.526 −3.856 1.00 14.64 A O ATOM 891 N SER A 149 31.589 70.512 −4.001 1.00 16.53 A N ATOM 892 CA SER A 149 32.681 71.102 −4.774 1.00 18.98 A C ATOM 893 CB SER A 149 33.875 70.146 −4.913 1.00 23.81 A C ATOM 894 OG SER A 149 33.494 68.992 −5.614 1.00 22.01 A O ATOM 895 C SER A 149 32.268 71.655 −6.141 1.00 18.12 A C ATOM 896 O SER A 149 32.865 72.619 −6.601 1.00 19.16 A O ATOM 897 N ALA A 150 31.242 71.083 −6.764 1.00 15.01 A N ATOM 898 CA ALA A 150 30.808 71.535 −8.085 1.00 19.55 A C ATOM 899 CB ALA A 150 29.875 70.524 −8.756 1.00 16.88 A C ATOM 900 C ALA A 150 30.149 72.905 −8.027 1.00 17.82 A C ATOM 901 O ALA A 150 30.080 73.600 −9.029 1.00 18.82 A O ATOM 902 N VAL A 151 29.714 73.304 −6.841 1.00 21.26 A N ATOM 903 CA VAL A 151 28.990 74.555 −6.679 1.00 21.12 A C ATOM 904 CB VAL A 151 27.551 74.294 −6.138 1.00 22.39 A C ATOM 905 CG1 VAL A 151 26.724 73.564 −7.191 1.00 15.09 A C ATOM 906 CG2 VAL A 151 27.589 73.488 −4.847 1.00 22.46 A C ATOM 907 C VAL A 151 29.726 75.561 −5.794 1.00 24.00 A C ATOM 908 O VAL A 151 29.165 76.590 −5.422 1.00 20.32 A O ATOM 909 N THR A 152 30.985 75.266 −5.461 1.00 19.95 A N ATOM 910 CA THR A 152 31.787 76.178 −4.653 1.00 22.13 A C ATOM 911 CB THR A 152 31.895 75.712 −3.177 1.00 22.56 A C ATOM 912 OG1 THR A 152 32.371 74.367 −3.132 1.00 24.29 A O ATOM 913 CG2 THR A 152 30.576 75.786 −2.480 1.00 22.50 A C ATOM 914 C THR A 152 33.199 76.271 −5.207 1.00 21.01 A C ATOM 915 O THR A 152 33.628 75.390 −5.958 1.00 21.18 A O ATOM 916 N PRO A 153 33.924 77.345 −4.853 1.00 23.41 A N ATOM 917 CD PRO A 153 33.424 78.620 −4.308 1.00 26.04 A C ATOM 918 CA PRO A 153 35.357 77.406 −5.154 1.00 25.29 A C ATOM 919 CB PRO A 153 35.703 78.880 −4.916 1.00 27.46 A C ATOM 920 CG PRO A 153 34.690 79.352 −3.953 1.00 29.44 A C ATOM 921 C PRO A 153 36.177 76.560 −4.193 1.00 28.79 A C ATOM 922 O PRO A 153 37.287 76.958 −3.860 1.00 30.08 A O ATOM 923 N LEU A 154 35.647 75.428 −3.746 1.00 28.02 A N ATOM 924 CA LEU A 154 36.356 74.583 −2.786 1.00 25.26 A C ATOM 925 CB LEU A 154 35.519 74.411 −1.510 1.00 23.27 A C ATOM 926 CG LEU A 154 35.060 75.704 −0.833 1.00 26.66 A C ATOM 927 CD1 LEU A 154 34.172 75.446 0.373 1.00 20.65 A C ATOM 928 CD2 LEU A 154 36.260 76.543 −0.442 1.00 21.94 A C ATOM 929 C LEU A 154 36.667 73.218 −3.376 1.00 23.28 A C ATOM 930 O LEU A 154 35.938 72.736 −4.251 1.00 19.71 A O ATOM 931 N THR A 155 37.754 72.606 −2.902 1.00 21.82 A N ATOM 932 CA THR A 155 38.078 71.216 −3.204 1.00 22.32 A C ATOM 933 CB THR A 155 39.382 71.052 −4.018 1.00 25.18 A C ATOM 934 OG1 THR A 155 40.504 71.342 −3.175 1.00 28.22 A O ATOM 935 CG2 THR A 155 39.399 71.963 −5.234 1.00 23.93 A C ATOM 936 C THR A 155 38.259 70.441 −1.894 1.00 21.67 A C ATOM 937 O THR A 155 38.593 71.008 −0.859 1.00 22.99 A O ATOM 938 N PHE A 156 38.035 69.138 −1.946 1.00 16.51 A N ATOM 939 CA PHE A 156 38.069 68.327 −0.751 1.00 19.08 A C ATOM 940 CB PHE A 156 36.664 67.789 −0.448 1.00 21.82 A C ATOM 941 CG PHE A 156 35.641 68.873 −0.291 1.00 14.85 A C ATOM 942 CD1 PHE A 156 34.723 69.134 −1.293 1.00 17.28 A C ATOM 943 CD2 PHE A 156 35.638 69.666 0.831 1.00 14.11 A C ATOM 944 CE1 PHE A 156 33.807 70.157 −1.163 1.00 16.58 A C ATOM 945 CE2 PHE A 156 34.729 70.688 0.968 1.00 20.33 A C ATOM 946 CZ PHE A 156 33.809 70.931 −0.030 1.00 16.27 A C ATOM 947 C PHE A 156 39.066 67.215 −1.003 1.00 17.66 A C ATOM 948 O PHE A 156 39.067 66.611 −2.067 1.00 22.61 A O ATOM 949 N THR A 157 39.943 66.968 −0.044 1.00 19.73 A N ATOM 950 CA THR A 157 41.010 66.015 −0.261 1.00 15.88 A C ATOM 951 CB THR A 157 42.369 66.742 −0.465 1.00 24.96 A C ATOM 952 OG1 THR A 157 42.304 67.586 −1.625 1.00 20.50 A O ATOM 953 CG2 THR A 157 43.490 65.735 −0.671 1.00 26.22 A C ATOM 954 C THR A 157 41.108 65.109 0.950 1.00 22.51 A C ATOM 955 O THR A 157 41.269 65.595 2.068 1.00 23.47 A O ATOM 956 N ARG A 158 41.018 63.799 0.735 1.00 24.17 A N ATOM 957 CA ARG A 158 41.112 62.840 1.844 1.00 28.87 A C ATOM 958 CB ARG A 158 40.607 61.452 1.418 1.00 21.39 A C ATOM 959 CG ARG A 158 40.527 60.423 2.547 1.00 22.64 A C ATOM 960 CD ARG A 158 40.130 59.037 2.041 1.00 22.61 A C ATOM 961 NE ARG A 158 40.122 58.055 3.125 1.00 27.27 A N ATOM 962 CZ ARG A 158 39.852 56.758 2.986 1.00 25.98 A C ATOM 963 NH1 ARG A 158 39.544 56.245 1.802 1.00 24.16 A N ATOM 964 NH2 ARG A 158 39.891 55.958 4.046 1.00 23.22 A N ATOM 965 C ARG A 158 42.546 62.743 2.377 1.00 25.83 A C ATOM 966 O ARG A 158 43.489 62.524 1.612 1.00 27.48 A O ATOM 967 N VAL A 159 42.699 62.926 3.685 1.00 29.22 A N ATOM 968 CA VAL A 159 43.993 62.759 4.357 1.00 28.73 A C ATOM 969 CB VAL A 159 44.488 64.082 4.959 1.00 28.39 A C ATOM 970 CG1 VAL A 159 44.775 65.083 3.852 1.00 23.39 A C ATOM 971 CG2 VAL A 159 43.465 64.634 5.951 1.00 28.13 A C ATOM 972 C VAL A 159 43.917 61.732 5.479 1.00 29.18 A C ATOM 973 O VAL A 159 42.921 61.007 5.623 1.00 30.14 A O ATOM 974 N TYR A 160 44.957 61.673 6.296 1.00 31.38 A N ATOM 975 CA TYR A 160 44.953 60.716 7.394 1.00 30.83 A C ATOM 976 CB TYR A 160 45.637 59.421 6.943 1.00 26.82 A C ATOM 977 CG TYR A 160 45.034 58.828 5.675 1.00 30.50 A C ATOM 978 CD1 TYR A 160 45.425 59.276 4.410 1.00 25.38 A C ATOM 979 CE1 TYR A 160 44.859 58.743 3.250 1.00 28.31 A C ATOM 980 CD2 TYR A 160 44.079 57.818 5.745 1.00 30.67 A C ATOM 981 CE2 TYR A 160 43.521 57.271 4.598 1.00 30.78 A C ATOM 982 CZ TYR A 160 43.910 57.741 3.357 1.00 31.93 A C ATOM 983 OH TYR A 160 43.349 57.192 2.236 1.00 29.22 A O ATOM 984 C TYR A 160 45.573 61.261 8.685 1.00 34.04 A C ATOM 985 O TYR A 160 46.532 60.693 9.194 1.00 44.70 A O ATOM 986 N SER A 161 45.018 62.351 9.215 1.00 36.71 A N ATOM 987 CA SER A 161 45.527 62.962 10.449 1.00 32.72 A C ATOM 988 CB SER A 161 46.819 63.740 10.168 1.00 40.57 A C ATOM 989 OG SER A 161 46.658 64.646 9.078 1.00 39.16 A O ATOM 990 C SER A 161 44.515 63.895 11.116 1.00 39.89 A C ATOM 991 O SER A 161 43.554 64.337 10.491 1.00 36.50 A O ATOM 992 N ARG A 162 44.756 64.214 12.385 1.00 33.48 A N ATOM 993 CA ARG A 162 43.918 65.157 13.127 1.00 39.43 A C ATOM 994 CB ARG A 162 44.330 65.171 14.605 1.00 42.01 A C ATOM 995 CG ARG A 162 45.575 66.031 14.863 1.00 44.84 A C ATOM 996 CD ARG A 162 46.168 65.824 16.253 1.00 50.09 A C ATOM 997 NE ARG A 162 46.783 64.507 16.395 1.00 52.45 A N ATOM 998 CZ ARG A 162 48.072 64.250 16.181 1.00 51.61 A C ATOM 999 NH1 ARG A 162 48.533 63.015 16.335 1.00 51.46 A N ATOM 1000 NH2 ARG A 162 48.899 65.225 15.812 1.00 39.55 A N ATOM 1001 C ARG A 162 44.046 66.576 12.549 1.00 36.20 A C ATOM 1002 O ARG A 162 43.399 67.522 13.012 1.00 40.05 A O ATOM 1003 N ASP A 163 44.917 66.713 11.556 1.00 42.73 A N ATOM 1004 CA ASP A 163 45.217 67.996 10.912 1.00 45.93 A C ATOM 1005 CB ASP A 163 46.588 67.911 10.238 1.00 41.96 A C ATOM 1006 CG ASP A 163 47.344 69.228 10.257 1.00 55.09 A C ATOM 1007 OD1 ASP A 163 46.792 70.250 10.715 1.00 59.47 A O ATOM 1008 OD2 ASP A 163 48.510 69.234 9.809 1.00 58.61 A O ATOM 1009 C ASP A 163 44.167 68.369 9.865 1.00 38.29 A C ATOM 1010 O ASP A 163 44.094 69.519 9.419 1.00 36.95 A O ATOM 1011 N ALA A 164 43.365 67.385 9.470 1.00 32.89 A N ATOM 1012 CA ALA A 164 42.277 67.600 8.532 1.00 23.19 A C ATOM 1013 CB ALA A 164 41.453 66.341 8.416 1.00 24.02 A C ATOM 1014 C ALA A 164 41.398 68.733 9.019 1.00 23.13 A C ATOM 1015 O ALA A 164 41.179 68.874 10.222 1.00 26.24 A O ATOM 1016 N ASP A 165 40.891 69.540 8.095 1.00 22.62 A N ATOM 1017 CA ASP A 165 39.921 70.573 8.455 1.00 23.86 A C ATOM 1018 CB ASP A 165 39.555 71.397 7.222 1.00 23.54 A C ATOM 1019 CG ASP A 165 40.737 72.176 6.672 1.00 23.48 A C ATOM 1020 OD1 ASP A 165 41.461 72.806 7.477 1.00 25.03 A O ATOM 1021 OD2 ASP A 165 40.941 72.157 5.441 1.00 20.18 A O ATOM 1022 C ASP A 165 38.671 69.911 9.019 1.00 23.22 A C ATOM 1023 O ASP A 165 38.095 70.360 10.011 1.00 24.16 A O ATOM 1024 N ILE A 166 38.286 68.820 8.374 1.00 26.16 A N ATOM 1025 CA ILE A 166 37.083 68.091 8.694 1.00 22.84 A C ATOM 1026 CB ILE A 166 36.175 68.003 7.450 1.00 21.31 A C ATOM 1027 CG2 ILE A 166 35.010 67.062 7.698 1.00 20.91 A C ATOM 1028 CG1 ILE A 166 35.659 69.402 7.076 1.00 17.04 A C ATOM 1029 CD1 ILE A 166 34.902 69.488 5.766 1.00 15.49 A C ATOM 1030 C ILE A 166 37.407 66.677 9.190 1.00 22.77 A C ATOM 1031 O ILE A 166 37.779 65.812 8.410 1.00 21.75 A O ATOM 1032 N VAL A 167 37.243 66.439 10.484 1.00 23.93 A N ATOM 1033 CA VAL A 167 37.380 65.084 11.003 1.00 24.64 A C ATOM 1034 CB VAL A 167 38.104 65.043 12.354 1.00 26.50 A C ATOM 1035 CG1 VAL A 167 38.240 63.597 12.832 1.00 26.08 A C ATOM 1036 CG2 VAL A 167 39.477 65.697 12.244 1.00 21.76 A C ATOM 1037 C VAL A 167 36.007 64.408 11.089 1.00 22.00 A C ATOM 1038 O VAL A 167 35.061 64.954 11.658 1.00 22.63 A O ATOM 1039 N ILE A 168 35.921 63.234 10.477 1.00 20.73 A N ATOM 1040 CA ILE A 168 34.695 62.459 10.356 1.00 20.64 A C ATOM 1041 CB ILE A 168 34.527 61.889 8.922 1.00 17.98 A C ATOM 1042 CG2 ILE A 168 33.370 60.871 8.874 1.00 22.07 A C ATOM 1043 CG1 ILE A 168 34.331 63.034 7.906 1.00 20.58 A C ATOM 1044 CD1 ILE A 168 34.342 62.626 6.434 1.00 18.81 A C ATOM 1045 C ILE A 168 34.777 61.303 11.344 1.00 21.36 A C ATOM 1046 O ILE A 168 35.805 60.637 11.430 1.00 17.41 A O ATOM 1047 N GLN A 169 33.688 61.055 12.063 1.00 18.99 A N ATOM 1048 CA GLN A 169 33.705 60.132 13.190 1.00 21.15 A C ATOM 1049 CB GLN A 169 34.006 60.945 14.454 1.00 22.26 A C ATOM 1050 CG GLN A 169 34.634 60.205 15.581 1.00 25.51 A C ATOM 1051 CD GLN A 169 34.727 61.067 16.833 1.00 31.76 A C ATOM 1052 OE1 GLN A 169 35.681 61.824 17.010 1.00 36.50 A O ATOM 1053 NE2 GLN A 169 33.725 60.960 17.702 1.00 29.33 A N ATOM 1054 C GLN A 169 32.351 59.444 13.352 1.00 20.36 A C ATOM 1055 O GLN A 169 31.312 60.086 13.255 1.00 17.36 A O ATOM 1056 N PHE A 170 32.369 58.131 13.557 1.00 15.98 A N ATOM 1057 CA PHE A 170 31.188 57.393 13.959 1.00 20.47 A C ATOM 1058 CB PHE A 170 31.150 56.031 13.249 1.00 20.08 A C ATOM 1059 CG PHE A 170 30.867 56.127 11.776 1.00 19.04 A C ATOM 1060 CD1 PHE A 170 31.908 56.211 10.850 1.00 21.45 A C ATOM 1061 CD2 PHE A 170 29.562 56.169 11.312 1.00 19.97 A C ATOM 1062 CE1 PHE A 170 31.641 56.312 9.503 1.00 20.80 A C ATOM 1063 CE2 PHE A 170 29.291 56.278 9.959 1.00 21.54 A C ATOM 1064 CZ PHE A 170 30.326 56.356 9.054 1.00 22.29 A C ATOM 1065 C PHE A 170 31.290 57.193 15.477 1.00 20.46 A C ATOM 1066 O PHE A 170 32.304 56.682 15.965 1.00 20.44 A O ATOM 1067 N GLY A 171 30.263 57.604 16.213 1.00 16.45 A N ATOM 1068 CA GLY A 171 30.231 57.431 17.664 1.00 21.87 A C ATOM 1069 C GLY A 171 28.841 57.114 18.199 1.00 24.66 A C ATOM 1070 O GLY A 171 27.859 57.165 17.450 1.00 24.42 A O ATOM 1071 N VAL A 172 28.752 56.763 19.484 1.00 23.94 A N ATOM 1072 CA VAL A 172 27.467 56.549 20.131 1.00 21.54 A C ATOM 1073 CB VAL A 172 27.153 55.052 20.311 1.00 19.09 A C ATOM 1074 CG1 VAL A 172 27.279 54.319 18.985 1.00 23.71 A C ATOM 1075 CG2 VAL A 172 28.047 54.434 21.387 1.00 20.03 A C ATOM 1076 C VAL A 172 27.410 57.207 21.506 1.00 24.46 A C ATOM 1077 O VAL A 172 28.443 57.496 22.125 1.00 21.92 A O ATOM 1078 N ALA A 173 26.192 57.405 21.990 1.00 25.40 A N ATOM 1079 CA ALA A 173 25.977 58.023 23.284 1.00 27.47 A C ATOM 1080 CB ALA A 173 26.108 56.993 24.398 1.00 18.62 A C ATOM 1081 C ALA A 173 27.018 59.116 23.435 1.00 26.51 A C ATOM 1082 O ALA A 173 27.181 59.940 22.532 1.00 22.93 A O ATOM 1083 N GLU A 174 27.726 59.126 24.567 1.00 25.79 A N ATOM 1084 CA GLU A 174 28.790 60.109 24.765 1.00 25.15 A C ATOM 1085 CB GLU A 174 29.057 60.374 26.249 1.00 28.27 A C ATOM 1086 CG GLU A 174 30.341 61.161 26.496 1.00 30.28 A C ATOM 1087 CD GLU A 174 30.341 62.511 25.800 1.00 29.38 A C ATOM 1088 OE1 GLU A 174 29.243 63.051 25.559 1.00 30.98 A O ATOM 1089 OE2 GLU A 174 31.437 63.041 25.502 1.00 35.72 A O ATOM 1090 C GLU A 174 30.075 59.680 24.061 1.00 28.92 A C ATOM 1091 O GLU A 174 30.625 58.608 24.327 1.00 29.37 A O ATOM 1092 N HIS A 175 30.569 60.527 23.170 1.00 27.57 A N ATOM 1093 CA HIS A 175 31.654 60.107 22.298 1.00 26.42 A C ATOM 1094 CB HIS A 175 31.128 59.795 20.901 1.00 25.80 A C ATOM 1095 CG HIS A 175 30.433 60.946 20.254 1.00 21.89 A C ATOM 1096 CD2 HIS A 175 30.850 61.834 19.321 1.00 25.03 A C ATOM 1097 ND1 HIS A 175 29.139 61.296 20.562 1.00 25.33 A N ATOM 1098 CE1 HIS A 175 28.782 62.345 19.842 1.00 24.26 A C ATOM 1099 NE2 HIS A 175 29.805 62.694 19.084 1.00 25.74 A N ATOM 1100 C HIS A 175 32.794 61.113 22.212 1.00 27.03 A C ATOM 1101 O HIS A 175 33.512 61.142 21.229 1.00 31.03 A O ATOM 1102 N GLY A 176 32.951 61.938 23.237 1.00 27.04 A N ATOM 1103 CA GLY A 176 34.168 62.709 23.374 1.00 26.17 A C ATOM 1104 C GLY A 176 34.046 64.183 23.082 1.00 26.62 A C ATOM 1105 O GLY A 176 35.063 64.869 23.002 1.00 31.64 A O ATOM 1106 N ASP A 177 32.823 64.681 22.913 1.00 25.02 A N ATOM 1107 CA ASP A 177 32.656 66.120 22.664 1.00 32.43 A C ATOM 1108 CB ASP A 177 32.493 66.409 21.172 1.00 30.69 A C ATOM 1109 CG ASP A 177 31.181 65.895 20.608 1.00 29.03 A C ATOM 1110 OD1 ASP A 177 30.301 65.460 21.387 1.00 26.59 A O ATOM 1111 OD2 ASP A 177 31.035 65.941 19.371 1.00 22.89 A O ATOM 1112 C ASP A 177 31.558 66.821 23.465 1.00 31.59 A C ATOM 1113 O ASP A 177 31.284 67.998 23.235 1.00 32.48 A O ATOM 1114 N GLY A 178 30.934 66.103 24.395 1.00 31.64 A N ATOM 1115 CA GLY A 178 29.968 66.707 25.302 1.00 29.02 A C ATOM 1116 C GLY A 178 28.656 67.051 24.629 1.00 28.26 A C ATOM 1117 O GLY A 178 27.855 67.832 25.145 1.00 25.98 A O ATOM 1118 N TYR A 179 28.447 66.466 23.455 1.00 27.08 A N ATOM 1119 CA TYR A 179 27.180 66.545 22.756 1.00 26.03 A C ATOM 1120 CB TYR A 179 27.313 67.416 21.519 1.00 29.37 A C ATOM 1121 CG TYR A 179 27.610 68.871 21.804 1.00 27.70 A C ATOM 1122 CD1 TYR A 179 28.908 69.364 21.750 1.00 31.62 A C ATOM 1123 CE1 TYR A 179 29.181 70.705 22.000 1.00 26.67 A C ATOM 1124 CD2 TYR A 179 26.586 69.751 22.115 1.00 28.47 A C ATOM 1125 CE2 TYR A 179 26.839 71.076 22.370 1.00 29.60 A C ATOM 1126 CZ TYR A 179 28.138 71.551 22.312 1.00 31.08 A C ATOM 1127 OH TYR A 179 28.370 72.881 22.563 1.00 34.24 A O ATOM 1128 C TYR A 179 26.820 65.123 22.367 1.00 27.64 A C ATOM 1129 O TYR A 179 26.949 64.736 21.208 1.00 30.56 A O ATOM 1130 N PRO A 180 26.384 64.331 23.350 1.00 30.40 A N ATOM 1131 CD PRO A 180 25.938 64.833 24.657 1.00 28.80 A C ATOM 1132 CA PRO A 180 26.185 62.884 23.224 1.00 28.18 A C ATOM 1133 CB PRO A 180 25.701 62.469 24.626 1.00 29.17 A C ATOM 1134 CG PRO A 180 25.999 63.609 25.507 1.00 33.85 A C ATOM 1135 C PRO A 180 25.092 62.543 22.236 1.00 23.80 A C ATOM 1136 O PRO A 180 24.120 63.284 22.106 1.00 25.16 A O ATOM 1137 N PHE A 181 25.221 61.405 21.576 1.00 23.75 A N ATOM 1138 CA PHE A 181 24.139 60.935 20.736 1.00 21.48 A C ATOM 1139 CB PHE A 181 24.646 59.990 19.635 1.00 20.65 A C ATOM 1140 CG PHE A 181 25.433 60.696 18.565 1.00 22.27 A C ATOM 1141 CD1 PHE A 181 24.922 61.838 17.959 1.00 23.26 A C ATOM 1142 CD2 PHE A 181 26.680 60.240 18.174 1.00 22.25 A C ATOM 1143 CE1 PHE A 181 25.640 62.509 16.986 1.00 24.95 A C ATOM 1144 CE2 PHE A 181 27.401 60.907 17.199 1.00 21.51 A C ATOM 1145 CZ PHE A 181 26.868 62.044 16.599 1.00 21.75 A C ATOM 1146 C PHE A 181 23.056 60.328 21.629 1.00 25.40 A C ATOM 1147 O PHE A 181 23.206 60.294 22.857 1.00 27.74 A O ATOM 1148 N ASP A 182 21.970 59.864 21.028 1.00 25.30 A N ATOM 1149 CA ASP A 182 20.772 59.531 21.795 1.00 24.75 A C ATOM 1150 CB ASP A 182 19.677 60.563 21.502 1.00 26.43 A C ATOM 1151 CG ASP A 182 19.255 60.557 20.041 1.00 23.66 A C ATOM 1152 OD1 ASP A 182 20.051 60.077 19.228 1.00 23.71 A O ATOM 1153 OD2 ASP A 182 18.150 61.038 19.693 1.00 24.88 A O ATOM 1154 C ASP A 182 20.220 58.116 21.535 1.00 24.89 A C ATOM 1155 O ASP A 182 19.043 57.850 21.794 1.00 27.79 A O ATOM 1156 N GLY A 183 21.059 57.216 21.026 1.00 28.78 A N ATOM 1157 CA GLY A 183 20.625 55.863 20.707 1.00 23.34 A C ATOM 1158 C GLY A 183 19.751 55.870 19.470 1.00 26.40 A C ATOM 1159 O GLY A 183 19.487 56.927 18.924 1.00 28.91 A O ATOM 1160 N LYS A 184 19.291 54.705 19.033 1.00 26.72 A N ATOM 1161 CA LYS A 184 18.527 54.585 17.788 1.00 26.75 A C ATOM 1162 CB LYS A 184 17.783 53.248 17.744 1.00 26.28 A C ATOM 1163 CG LYS A 184 17.536 52.738 16.326 1.00 35.08 A C ATOM 1164 CD LYS A 184 16.824 51.397 16.316 1.00 26.86 A C ATOM 1165 CE LYS A 184 15.321 51.594 16.222 1.00 41.57 A C ATOM 1166 NZ LYS A 184 14.921 52.092 14.870 1.00 31.43 A N ATOM 1167 C LYS A 184 17.538 55.745 17.534 1.00 30.13 A C ATOM 1168 O LYS A 184 16.801 56.142 18.430 1.00 28.80 A O ATOM 1169 N ASP A 185 17.551 56.275 16.307 1.00 30.45 A N ATOM 1170 CA ASP A 185 16.660 57.367 15.876 1.00 26.69 A C ATOM 1171 CB ASP A 185 15.197 56.930 15.905 1.00 26.70 A C ATOM 1172 CG ASP A 185 14.956 55.681 15.092 1.00 30.55 A C ATOM 1173 OD1 ASP A 185 15.399 55.635 13.914 1.00 28.80 A O ATOM 1174 OD2 ASP A 185 14.331 54.742 15.630 1.00 30.45 A O ATOM 1175 C ASP A 185 16.855 58.676 16.642 1.00 26.48 A C ATOM 1176 O ASP A 185 17.875 58.882 17.261 1.00 28.97 A O ATOM 1177 N GLY A 186 15.874 59.569 16.609 1.00 27.98 A N ATOM 1178 CA GLY A 186 16.090 60.883 17.192 1.00 25.10 A C ATOM 1179 C GLY A 186 17.177 61.591 16.393 1.00 21.86 A C ATOM 1180 O GLY A 186 17.041 61.743 15.180 1.00 24.55 A O ATOM 1181 N LEU A 187 18.256 62.006 17.054 1.00 20.45 A N ATOM 1182 CA LEU A 187 19.370 62.689 16.371 1.00 24.60 A C ATOM 1183 CB LEU A 187 20.355 63.292 17.383 1.00 20.25 A C ATOM 1184 CG LEU A 187 19.797 64.154 18.501 1.00 31.73 A C ATOM 1185 CD1 LEU A 187 20.934 64.715 19.345 1.00 27.75 A C ATOM 1186 CD2 LEU A 187 18.991 65.260 17.882 1.00 28.29 A C ATOM 1187 C LEU A 187 20.139 61.685 15.569 1.00 23.90 A C ATOM 1188 O LEU A 187 20.523 60.665 16.116 1.00 24.81 A O ATOM 1189 N LEU A 188 20.410 61.983 14.300 1.00 17.67 A N ATOM 1190 CA LEU A 188 21.114 61.051 13.424 1.00 24.25 A C ATOM 1191 CB LEU A 188 20.531 61.093 12.012 1.00 16.41 A C ATOM 1192 CG LEU A 188 19.035 60.808 11.896 1.00 16.39 A C ATOM 1193 CD1 LEU A 188 18.563 61.034 10.457 1.00 19.02 A C ATOM 1194 CD2 LEU A 188 18.724 59.401 12.334 1.00 19.43 A C ATOM 1195 C LEU A 188 22.600 61.362 13.345 1.00 20.59 A C ATOM 1196 O LEU A 188 23.420 60.480 13.115 1.00 20.66 A O ATOM 1197 N ALA A 189 22.939 62.630 13.529 1.00 21.50 A N ATOM 1198 CA ALA A 189 24.299 63.079 13.305 1.00 21.34 A C ATOM 1199 CB ALA A 189 24.676 62.906 11.813 1.00 16.40 A C ATOM 1200 C ALA A 189 24.429 64.538 13.705 1.00 18.84 A C ATOM 1201 O ALA A 189 23.437 65.228 13.935 1.00 20.92 A O ATOM 1202 N HIS A 190 25.657 65.024 13.791 1.00 22.95 A N ATOM 1203 CA HIS A 190 25.837 66.464 13.922 1.00 20.72 A C ATOM 1204 CB HIS A 190 25.577 66.965 15.342 1.00 22.21 A C ATOM 1205 CG HIS A 190 26.439 66.344 16.391 1.00 20.39 A C ATOM 1206 CD2 HIS A 190 27.660 65.767 16.326 1.00 24.43 A C ATOM 1207 ND1 HIS A 190 26.062 66.297 17.715 1.00 24.65 A N ATOM 1208 CE1 HIS A 190 27.008 65.707 18.420 1.00 26.85 A C ATOM 1209 NE2 HIS A 190 27.982 65.364 17.599 1.00 23.35 A N ATOM 1210 C HIS A 190 27.188 66.908 13.416 1.00 22.43 A C ATOM 1211 O HIS A 190 28.005 66.081 13.008 1.00 20.43 A O ATOM 1212 N ALA A 191 27.406 68.219 13.415 1.00 18.09 A N ATOM 1213 CA ALA A 191 28.596 68.769 12.784 1.00 23.36 A C ATOM 1214 CB ALA A 191 28.425 68.806 11.258 1.00 21.01 A C ATOM 1215 C ALA A 191 28.839 70.161 13.318 1.00 21.11 A C ATOM 1216 O ALA A 191 27.946 70.761 13.891 1.00 22.47 A O ATOM 1217 N PHE A 192 30.050 70.667 13.116 1.00 21.67 A N ATOM 1218 CA PHE A 192 30.451 71.971 13.635 1.00 26.13 A C ATOM 1219 CB PHE A 192 31.518 71.769 14.723 1.00 25.80 A C ATOM 1220 CG PHE A 192 31.134 70.712 15.739 1.00 23.93 A C ATOM 1221 CD1 PHE A 192 30.282 71.017 16.792 1.00 27.38 A C ATOM 1222 CD2 PHE A 192 31.574 69.402 15.600 1.00 27.60 A C ATOM 1223 CE1 PHE A 192 29.889 70.040 17.703 1.00 26.70 A C ATOM 1224 CE2 PHE A 192 31.190 68.422 16.516 1.00 29.79 A C ATOM 1225 CZ PHE A 192 30.357 68.745 17.572 1.00 26.29 A C ATOM 1226 C PHE A 192 30.934 72.912 12.515 1.00 24.39 A C ATOM 1227 O PHE A 192 31.520 72.471 11.520 1.00 19.81 A O ATOM 1228 N PRO A 193 30.674 74.215 12.673 1.00 22.54 A N ATOM 1229 CD PRO A 193 30.110 74.812 13.898 1.00 19.32 A C ATOM 1230 CA PRO A 193 30.993 75.238 11.664 1.00 19.16 A C ATOM 1231 CB PRO A 193 30.422 76.515 12.286 1.00 23.22 A C ATOM 1232 CG PRO A 193 30.485 76.256 13.758 1.00 28.21 A C ATOM 1233 C PRO A 193 32.495 75.378 11.469 1.00 24.38 A C ATOM 1234 O PRO A 193 33.245 75.121 12.413 1.00 24.91 A O ATOM 1235 N PRO A 194 32.930 75.785 10.260 1.00 29.17 A N ATOM 1236 CD PRO A 194 32.086 76.297 9.164 1.00 22.00 A C ATOM 1237 CA PRO A 194 34.361 75.866 9.938 1.00 22.91 A C ATOM 1238 CB PRO A 194 34.383 76.672 8.640 1.00 22.42 A C ATOM 1239 CG PRO A 194 33.054 76.432 8.017 1.00 23.54 A C ATOM 1240 C PRO A 194 35.131 76.599 11.022 1.00 22.56 A C ATOM 1241 O PRO A 194 34.621 77.567 11.586 1.00 26.04 A O ATOM 1242 N GLY A 195 36.328 76.117 11.328 1.00 22.70 A N ATOM 1243 CA GLY A 195 37.185 76.782 12.284 1.00 23.27 A C ATOM 1244 C GLY A 195 38.234 75.848 12.857 1.00 30.20 A C ATOM 1245 O GLY A 195 38.473 74.769 12.319 1.00 27.56 A O ATOM 1246 N PRO A 196 38.860 76.259 13.967 1.00 25.85 A N ATOM 1247 CD PRO A 196 38.541 77.505 14.674 1.00 29.35 A C ATOM 1248 CA PRO A 196 39.933 75.506 14.622 1.00 32.15 A C ATOM 1249 CB PRO A 196 40.544 76.525 15.591 1.00 29.63 A C ATOM 1250 CG PRO A 196 39.814 77.827 15.362 1.00 33.83 A C ATOM 1251 C PRO A 196 39.400 74.341 15.443 1.00 34.18 A C ATOM 1252 O PRO A 196 38.258 74.383 15.914 1.00 31.65 A O ATOM 1253 N GLY A 197 40.242 73.331 15.633 1.00 28.73 A N ATOM 1254 CA GLY A 197 39.962 72.265 16.572 1.00 35.57 A C ATOM 1255 C GLY A 197 38.790 71.426 16.128 1.00 37.34 A C ATOM 1256 O GLY A 197 38.791 70.921 15.016 1.00 30.91 A O ATOM 1257 N ILE A 198 37.779 71.288 16.981 1.00 25.71 A N ATOM 1258 CA ILE A 198 36.635 70.459 16.622 1.00 30.08 A C ATOM 1259 CB ILE A 198 35.768 70.110 17.825 1.00 28.72 A C ATOM 1260 CG2 ILE A 198 34.847 71.268 18.179 1.00 31.56 A C ATOM 1261 CG1 ILE A 198 34.959 68.851 17.532 1.00 31.98 A C ATOM 1262 CD1 ILE A 198 33.786 68.685 18.420 1.00 30.63 A C ATOM 1263 C ILE A 198 35.753 71.108 15.554 1.00 30.39 A C ATOM 1264 O ILE A 198 34.929 70.439 14.924 1.00 31.90 A O ATOM 1265 N GLN A 199 35.908 72.410 15.352 1.00 31.18 A N ATOM 1266 CA GLN A 199 35.105 73.073 14.339 1.00 29.84 A C ATOM 1267 CB GLN A 199 35.352 74.579 14.370 1.00 25.60 A C ATOM 1268 CG GLN A 199 34.920 75.144 15.718 1.00 28.40 A C ATOM 1269 CD GLN A 199 34.975 76.647 15.815 1.00 31.87 A C ATOM 1270 OE1 GLN A 199 34.604 77.355 14.880 1.00 29.19 A O ATOM 1271 NE2 GLN A 199 35.420 77.149 16.970 1.00 26.73 A N ATOM 1272 C GLN A 199 35.366 72.418 12.986 1.00 29.89 A C ATOM 1273 O GLN A 199 36.479 71.976 12.717 1.00 27.68 A O ATOM 1274 N GLY A 200 34.323 72.310 12.163 1.00 26.78 A N ATOM 1275 CA GLY A 200 34.416 71.606 10.896 1.00 21.24 A C ATOM 1276 C GLY A 200 34.180 70.091 10.944 1.00 25.64 A C ATOM 1277 O GLY A 200 34.025 69.433 9.897 1.00 18.55 A O ATOM 1278 N ASP A 201 34.161 69.518 12.143 1.00 24.11 A N ATOM 1279 CA ASP A 201 33.989 68.073 12.263 1.00 20.38 A C ATOM 1280 CB ASP A 201 34.490 67.580 13.624 1.00 26.18 A C ATOM 1281 CG ASP A 201 35.981 67.665 13.734 1.00 24.98 A C ATOM 1282 OD1 ASP A 201 36.605 67.919 12.683 1.00 27.56 A O ATOM 1283 OD2 ASP A 201 36.520 67.497 14.849 1.00 22.34 A O ATOM 1284 C ASP A 201 32.549 67.620 12.060 1.00 21.02 A C ATOM 1285 O ASP A 201 31.613 68.378 12.297 1.00 19.68 A O ATOM 1286 N ALA A 202 32.395 66.365 11.650 1.00 20.34 A N ATOM 1287 CA ALA A 202 31.093 65.782 11.383 1.00 19.03 A C ATOM 1288 CB ALA A 202 30.919 65.596 9.865 1.00 16.44 A C ATOM 1289 C ALA A 202 30.977 64.435 12.092 1.00 17.95 A C ATOM 1290 O ALA A 202 31.754 63.527 11.818 1.00 20.14 A O ATOM 1291 N HIS A 203 30.008 64.296 12.983 1.00 18.96 A N ATOM 1292 CA HIS A 203 29.849 63.040 13.715 1.00 22.20 A C ATOM 1293 CB HIS A 203 29.923 63.290 15.225 1.00 20.47 A C ATOM 1294 CG HIS A 203 31.199 63.937 15.666 1.00 18.78 A C ATOM 1295 CD2 HIS A 203 32.321 64.256 14.978 1.00 23.70 A C ATOM 1296 ND1 HIS A 203 31.422 64.340 16.966 1.00 27.81 A N ATOM 1297 CE1 HIS A 203 32.622 64.885 17.058 1.00 27.49 A C ATOM 1298 NE2 HIS A 203 33.186 64.850 15.865 1.00 22.82 A N ATOM 1299 C HIS A 203 28.546 62.329 13.345 1.00 23.25 A C ATOM 1300 O HIS A 203 27.489 62.963 13.203 1.00 19.33 A O ATOM 1301 N PHE A 204 28.633 61.010 13.198 1.00 19.60 A N ATOM 1302 CA PHE A 204 27.492 60.199 12.779 1.00 21.49 A C ATOM 1303 CB PHE A 204 27.821 59.516 11.456 1.00 21.59 A C ATOM 1304 CG PHE A 204 28.095 60.485 10.334 1.00 22.75 A C ATOM 1305 CD1 PHE A 204 29.365 61.003 10.129 1.00 19.92 A C ATOM 1306 CD2 PHE A 204 27.067 60.901 9.512 1.00 19.75 A C ATOM 1307 CE1 PHE A 204 29.617 61.912 9.092 1.00 19.21 A C ATOM 1308 CE2 PHE A 204 27.294 61.801 8.479 1.00 15.45 A C ATOM 1309 CZ PHE A 204 28.571 62.312 8.266 1.00 17.79 A C ATOM 1310 C PHE A 204 27.139 59.163 13.846 1.00 22.85 A C ATOM 1311 O PHE A 204 28.011 58.429 14.314 1.00 19.45 A O ATOM 1312 N ASP A 205 25.860 59.117 14.230 1.00 23.70 A N ATOM 1313 CA ASP A 205 25.403 58.305 15.362 1.00 19.94 A C ATOM 1314 CB ASP A 205 24.048 58.820 15.874 1.00 23.02 A C ATOM 1315 CG ASP A 205 23.531 58.044 17.097 1.00 24.12 A C ATOM 1316 OD1 ASP A 205 24.156 57.055 17.522 1.00 23.68 A O ATOM 1317 OD2 ASP A 205 22.492 58.438 17.652 1.00 19.54 A O ATOM 1318 C ASP A 205 25.300 56.842 14.972 1.00 22.65 A C ATOM 1319 O ASP A 205 24.382 56.439 14.236 1.00 24.59 A O ATOM 1320 N ASP A 206 26.233 56.040 15.471 1.00 21.76 A N ATOM 1321 CA ASP A 206 26.348 54.682 14.988 1.00 22.23 A C ATOM 1322 CB ASP A 206 27.761 54.146 15.171 1.00 20.72 A C ATOM 1323 CG ASP A 206 28.092 53.036 14.187 1.00 18.65 A C ATOM 1324 OD1 ASP A 206 27.285 52.770 13.271 1.00 22.02 A O ATOM 1325 OD2 ASP A 206 29.175 52.433 14.326 1.00 22.24 A O ATOM 1326 C ASP A 206 25.346 53.774 15.663 1.00 23.45 A C ATOM 1327 O ASP A 206 25.384 52.577 15.466 1.00 24.62 A O ATOM 1328 N ASP A 207 24.461 54.346 16.473 1.00 22.69 A N ATOM 1329 CA ASP A 207 23.316 53.601 16.967 1.00 22.44 A C ATOM 1330 CB ASP A 207 22.773 54.212 18.276 1.00 23.50 A C ATOM 1331 CG ASP A 207 23.460 53.648 19.527 1.00 26.19 A C ATOM 1332 OD1 ASP A 207 24.074 52.571 19.436 1.00 19.67 A O ATOM 1333 OD2 ASP A 207 23.380 54.277 20.606 1.00 24.21 A O ATOM 1334 C ASP A 207 22.229 53.549 15.892 1.00 22.53 A C ATOM 1335 O ASP A 207 21.194 52.909 16.077 1.00 26.89 A O ATOM 1336 N GLU A 208 22.450 54.235 14.771 1.00 22.42 A N ATOM 1337 CA GLU A 208 21.602 54.035 13.595 1.00 19.67 A C ATOM 1338 CB GLU A 208 21.558 55.279 12.722 1.00 22.24 A C ATOM 1339 CG GLU A 208 21.338 56.558 13.437 1.00 19.10 A C ATOM 1340 CD GLU A 208 20.128 56.522 14.310 1.00 21.30 A C ATOM 1341 OE1 GLU A 208 19.215 55.715 14.030 1.00 23.81 A O ATOM 1342 OE2 GLU A 208 20.086 57.306 15.286 1.00 25.29 A O ATOM 1343 C GLU A 208 22.194 52.947 12.730 1.00 21.97 A C ATOM 1344 O GLU A 208 23.410 52.811 12.669 1.00 24.08 A O ATOM 1345 N LEU A 209 21.332 52.203 12.040 1.00 17.26 A N ATOM 1346 CA LEU A 209 21.743 51.370 10.921 1.00 23.11 A C ATOM 1347 CB LEU A 209 20.619 50.405 10.513 1.00 19.69 A C ATOM 1348 CG LEU A 209 20.855 49.552 9.252 1.00 22.75 A C ATOM 1349 CD1 LEU A 209 21.952 48.533 9.519 1.00 20.86 A C ATOM 1350 CD2 LEU A 209 19.567 48.860 8.761 1.00 20.19 A C ATOM 1351 C LEU A 209 22.034 52.299 9.748 1.00 22.51 A C ATOM 1352 O LEU A 209 21.125 52.943 9.237 1.00 19.37 A O ATOM 1353 N TRP A 210 23.293 52.380 9.332 1.00 24.64 A N ATOM 1354 CA TRP A 210 23.635 53.141 8.133 1.00 21.60 A C ATOM 1355 CB TRP A 210 24.999 53.833 8.283 1.00 23.45 A C ATOM 1356 CG TRP A 210 24.970 54.842 9.392 1.00 23.31 A C ATOM 1357 CD2 TRP A 210 24.338 56.129 9.367 1.00 25.13 A C ATOM 1358 CE2 TRP A 210 24.537 56.714 10.629 1.00 23.45 A C ATOM 1359 CE3 TRP A 210 23.637 56.848 8.393 1.00 22.49 A C ATOM 1360 CD1 TRP A 210 25.488 54.696 10.644 1.00 23.29 A C ATOM 1361 NE1 TRP A 210 25.244 55.821 11.390 1.00 20.62 A N ATOM 1362 CZ2 TRP A 210 24.049 57.986 10.948 1.00 23.89 A C ATOM 1363 CZ3 TRP A 210 23.158 58.103 8.711 1.00 21.43 A C ATOM 1364 CH2 TRP A 210 23.380 58.667 9.967 1.00 16.83 A C ATOM 1365 C TRP A 210 23.594 52.257 6.893 1.00 27.23 A C ATOM 1366 O TRP A 210 24.038 51.101 6.918 1.00 23.47 A O ATOM 1367 N SER A 211 23.022 52.808 5.826 1.00 25.99 A N ATOM 1368 CA SER A 211 22.995 52.162 4.520 1.00 23.44 A C ATOM 1369 CB SER A 211 21.750 51.279 4.370 1.00 21.90 A C ATOM 1370 OG SER A 211 20.552 52.052 4.396 1.00 20.73 A O ATOM 1371 C SER A 211 23.001 53.243 3.447 1.00 22.35 A C ATOM 1372 O SER A 211 23.518 54.347 3.657 1.00 18.50 A O ATOM 1373 N LEU A 212 22.425 52.932 2.292 1.00 24.80 A N ATOM 1374 CA LEU A 212 22.223 53.955 1.287 1.00 27.49 A C ATOM 1375 CB LEU A 212 22.809 53.529 −0.055 1.00 24.56 A C ATOM 1376 CG LEU A 212 24.330 53.402 0.044 1.00 27.84 A C ATOM 1377 CD1 LEU A 212 24.992 53.043 −1.291 1.00 28.51 A C ATOM 1378 CD2 LEU A 212 24.912 54.693 0.610 1.00 23.59 A C ATOM 1379 C LEU A 212 20.756 54.391 1.174 1.00 27.71 A C ATOM 1380 O LEU A 212 20.349 54.936 0.153 1.00 27.60 A O ATOM 1381 N GLY A 213 19.982 54.158 2.235 1.00 26.13 A N ATOM 1382 CA GLY A 213 18.612 54.648 2.335 1.00 26.04 A C ATOM 1383 C GLY A 213 17.517 53.792 1.700 1.00 31.54 A C ATOM 1384 O GLY A 213 16.324 54.013 1.938 1.00 26.88 A O ATOM 1385 N LYS A 389 17.915 52.828 0.879 1.00 31.49 A N ATOM 1386 CA LYS A 389 16.964 51.890 0.298 1.00 33.93 A C ATOM 1387 CB LYS A 389 17.379 51.488 −1.111 1.00 36.04 A C ATOM 1388 CG LYS A 389 17.116 52.553 −2.151 1.00 40.69 A C ATOM 1389 CD LYS A 389 15.619 52.827 −2.276 1.00 45.66 A C ATOM 1390 CE LYS A 389 14.884 51.640 −2.897 1.00 50.54 A C ATOM 1391 NZ LYS A 389 13.457 51.966 −3.186 1.00 50.29 A N ATOM 1392 C LYS A 389 16.834 50.642 1.153 1.00 35.52 A C ATOM 1393 O LYS A 389 17.830 50.101 1.643 1.00 30.72 A O ATOM 1394 N GLY A 390 15.595 50.195 1.312 1.00 29.44 A N ATOM 1395 CA GLY A 390 15.293 48.971 2.027 1.00 32.26 A C ATOM 1396 C GLY A 390 15.127 49.211 3.512 1.00 33.50 A C ATOM 1397 O GLY A 390 14.021 49.120 4.053 1.00 44.73 A O ATOM 1398 N GLN A 391 16.234 49.496 4.181 1.00 28.66 A N ATOM 1399 CA GLN A 391 16.227 49.742 5.617 1.00 29.78 A C ATOM 1400 CB GLN A 391 16.327 48.421 6.399 1.00 30.83 A C ATOM 1401 CG GLN A 391 15.479 47.268 5.844 1.00 31.95 A C ATOM 1402 CD GLN A 391 15.385 46.078 6.787 1.00 32.46 A C ATOM 1403 OE1 GLN A 391 15.724 46.173 7.968 1.00 33.53 A O ATOM 1404 NE2 GLN A 391 14.908 44.950 6.268 1.00 41.33 A N ATOM 1405 C GLN A 391 17.424 50.624 5.946 1.00 26.24 A C ATOM 1406 O GLN A 391 18.430 50.592 5.236 1.00 27.65 A O ATOM 1407 N GLY A 392 17.310 51.413 7.012 1.00 23.37 A N ATOM 1408 CA GLY A 392 18.429 52.183 7.523 1.00 20.75 A C ATOM 1409 C GLY A 392 18.471 53.588 6.951 1.00 26.82 A C ATOM 1410 O GLY A 392 17.734 53.910 6.011 1.00 22.43 A O ATOM 1411 N TYR A 393 19.337 54.427 7.511 1.00 21.44 A N ATOM 1412 CA TYR A 393 19.488 55.797 7.012 1.00 23.82 A C ATOM 1413 CB TYR A 393 19.759 56.765 8.164 1.00 22.67 A C ATOM 1414 CG TYR A 393 18.634 56.845 9.164 1.00 22.03 A C ATOM 1415 CD1 TYR A 393 17.542 57.698 8.958 1.00 22.60 A C ATOM 1416 CE1 TYR A 393 16.504 57.770 9.884 1.00 22.47 A C ATOM 1417 CD2 TYR A 393 18.657 56.074 10.329 1.00 26.89 A C ATOM 1418 CE2 TYR A 393 17.623 56.146 11.257 1.00 24.45 A C ATOM 1419 CZ TYR A 393 16.556 56.995 11.029 1.00 23.23 A C ATOM 1420 OH TYR A 393 15.535 57.055 11.963 1.00 30.46 A O ATOM 1421 C TYR A 393 20.600 55.907 5.988 1.00 22.06 A C ATOM 1422 O TYR A 393 21.663 55.306 6.159 1.00 21.23 A O ATOM 1423 N SER A 394 20.355 56.677 4.926 1.00 20.20 A N ATOM 1424 CA SER A 394 21.381 56.940 3.933 1.00 22.18 A C ATOM 1425 CB SER A 394 20.808 57.702 2.722 1.00 19.88 A C ATOM 1426 OG SER A 394 21.860 58.105 1.856 1.00 17.16 A O ATOM 1427 C SER A 394 22.533 57.749 4.509 1.00 18.58 A C ATOM 1428 O SER A 394 22.377 58.923 4.849 1.00 18.50 A O ATOM 1429 N LEU A 395 23.698 57.126 4.592 1.00 16.64 A N ATOM 1430 CA LEU A 395 24.920 57.840 4.911 1.00 19.19 A C ATOM 1431 CB LEU A 395 26.060 56.839 5.004 1.00 20.92 A C ATOM 1432 CG LEU A 395 27.405 57.412 5.419 1.00 15.52 A C ATOM 1433 CD1 LEU A 395 27.309 58.000 6.798 1.00 18.24 A C ATOM 1434 CD2 LEU A 395 28.419 56.284 5.382 1.00 16.12 A C ATOM 1435 C LEU A 395 25.299 58.920 3.883 1.00 20.72 A C ATOM 1436 O LEU A 395 25.887 59.948 4.226 1.00 17.03 A O ATOM 1437 N PHE A 396 25.020 58.668 2.612 1.00 19.09 A N ATOM 1438 CA PHE A 396 25.335 59.646 1.587 1.00 14.85 A C ATOM 1439 CB PHE A 396 25.028 59.073 0.196 1.00 16.67 A C ATOM 1440 CG PHE A 396 24.979 60.102 −0.900 1.00 18.43 A C ATOM 1441 CD1 PHE A 396 26.044 60.976 −1.116 1.00 16.10 A C ATOM 1442 CD2 PHE A 396 23.882 60.165 −1.747 1.00 19.50 A C ATOM 1443 CE1 PHE A 396 25.988 61.914 −2.137 1.00 17.21 A C ATOM 1444 CE2 PHE A 396 23.829 61.105 −2.779 1.00 17.18 A C ATOM 1445 CZ PHE A 396 24.868 61.980 −2.966 1.00 16.87 A C ATOM 1446 C PHE A 396 24.580 60.959 1.847 1.00 17.39 A C ATOM 1447 O PHE A 396 25.187 62.022 1.872 1.00 15.92 A O ATOM 1448 N LEU A 397 23.268 60.879 2.070 1.00 14.77 A N ATOM 1449 CA LEU A 397 22.436 62.090 2.251 1.00 18.57 A C ATOM 1450 CB LEU A 397 20.945 61.756 2.114 1.00 10.89 A C ATOM 1451 CG LEU A 397 20.395 61.299 0.763 1.00 16.80 A C ATOM 1452 CD1 LEU A 397 19.022 60.664 0.921 1.00 14.99 A C ATOM 1453 CD2 LEU A 397 20.359 62.464 −0.238 1.00 16.45 A C ATOM 1454 C LEU A 397 22.675 62.803 3.592 1.00 16.09 A C ATOM 1455 O LEU A 397 22.695 64.033 3.662 1.00 16.68 A O ATOM 1456 N VAL A 398 22.822 62.030 4.659 1.00 13.58 A N ATOM 1457 CA VAL A 398 23.151 62.601 5.968 1.00 11.85 A C ATOM 1458 CB VAL A 398 23.104 61.544 7.112 1.00 18.88 A C ATOM 1459 CG1 VAL A 398 23.622 62.122 8.402 1.00 15.54 A C ATOM 1460 CG2 VAL A 398 21.672 61.023 7.310 1.00 18.70 A C ATOM 1461 C VAL A 398 24.513 63.274 5.925 1.00 17.07 A C ATOM 1462 O VAL A 398 24.664 64.397 6.422 1.00 17.67 A O ATOM 1463 N ALA A 399 25.508 62.597 5.343 1.00 16.28 A N ATOM 1464 CA ALA A 399 26.814 63.214 5.143 1.00 21.17 A C ATOM 1465 CB ALA A 399 27.797 62.248 4.481 1.00 13.68 A C ATOM 1466 C ALA A 399 26.726 64.519 4.339 1.00 18.09 A C ATOM 1467 O ALA A 399 27.328 65.520 4.718 1.00 22.97 A O ATOM 1468 N ALA A 400 25.993 64.510 3.233 1.00 15.39 A N ATOM 1469 CA ALA A 400 25.894 65.714 2.409 1.00 14.82 A C ATOM 1470 CB ALA A 400 25.043 65.458 1.184 1.00 14.15 A C ATOM 1471 C ALA A 400 25.340 66.891 3.232 1.00 18.84 A C ATOM 1472 O ALA A 400 25.832 68.024 3.135 1.00 16.89 A O ATOM 1473 N HIS A 401 24.327 66.614 4.048 1.00 16.48 A N ATOM 1474 CA HIS A 401 23.727 67.641 4.911 1.00 14.00 A C ATOM 1475 CB HIS A 401 22.417 67.127 5.527 1.00 14.73 A C ATOM 1476 CG HIS A 401 21.875 67.968 6.646 1.00 14.40 A C ATOM 1477 CD2 HIS A 401 22.265 68.099 7.942 1.00 16.05 A C ATOM 1478 ND1 HIS A 401 20.771 68.780 6.499 1.00 13.21 A N ATOM 1479 CE1 HIS A 401 20.504 69.382 7.644 1.00 14.56 A C ATOM 1480 NE2 HIS A 401 21.399 68.993 8.536 1.00 15.39 A N ATOM 1481 C HIS A 401 24.727 68.102 5.965 1.00 14.98 A C ATOM 1482 O HIS A 401 24.928 69.303 6.140 1.00 14.19 A O ATOM 1483 N GLU A 402 25.382 67.150 6.633 1.00 13.72 A N ATOM 1484 CA GLU A 402 26.338 67.489 7.673 1.00 17.13 A C ATOM 1485 CB GLU A 402 26.778 66.248 8.459 1.00 18.13 A C ATOM 1486 CG GLU A 402 25.642 65.519 9.133 1.00 20.00 A C ATOM 1487 CD GLU A 402 24.947 66.325 10.221 1.00 21.44 A C ATOM 1488 OE1 GLU A 402 25.441 67.409 10.608 1.00 16.77 A O ATOM 1489 OE2 GLU A 402 23.905 65.846 10.717 1.00 19.15 A O ATOM 1490 C GLU A 402 27.553 68.251 7.154 1.00 16.87 A C ATOM 1491 O GLU A 402 28.076 69.126 7.844 1.00 21.18 A O ATOM 1492 N PHE A 403 27.999 67.929 5.943 1.00 22.04 A N ATOM 1493 CA PHE A 403 29.135 68.628 5.344 1.00 17.59 A C ATOM 1494 CB PHE A 403 29.607 67.908 4.081 1.00 18.84 A C ATOM 1495 CG PHE A 403 30.211 66.547 4.344 1.00 15.71 A C ATOM 1496 CD1 PHE A 403 30.533 66.152 5.640 1.00 18.70 A C ATOM 1497 CD2 PHE A 403 30.462 65.673 3.304 1.00 15.16 A C ATOM 1498 CE1 PHE A 403 31.084 64.894 5.885 1.00 21.21 A C ATOM 1499 CE2 PHE A 403 31.025 64.434 3.527 1.00 18.09 A C ATOM 1500 CZ PHE A 403 31.331 64.032 4.827 1.00 18.47 A C ATOM 1501 C PHE A 403 28.802 70.099 5.051 1.00 19.68 A C ATOM 1502 O PHE A 403 29.678 70.954 5.086 1.00 19.50 A O ATOM 1503 N GLY A 404 27.537 70.374 4.748 1.00 19.48 A N ATOM 1504 CA GLY A 404 27.058 71.738 4.590 1.00 21.80 A C ATOM 1505 C GLY A 404 27.250 72.589 5.836 1.00 19.26 A C ATOM 1506 O GLY A 404 27.681 73.748 5.751 1.00 16.35 A O ATOM 1507 N HIS A 405 26.935 72.026 6.999 1.00 16.52 A N ATOM 1508 CA HIS A 405 27.262 72.708 8.253 1.00 19.54 A C ATOM 1509 CB HIS A 405 26.822 71.907 9.494 1.00 14.74 A C ATOM 1510 CG HIS A 405 25.348 71.859 9.698 1.00 17.78 A C ATOM 1511 CD2 HIS A 405 24.528 70.834 10.038 1.00 12.73 A C ATOM 1512 ND1 HIS A 405 24.544 72.973 9.589 1.00 16.78 A N ATOM 1513 CE1 HIS A 405 23.293 72.632 9.835 1.00 19.11 A C ATOM 1514 NE2 HIS A 405 23.260 71.341 10.112 1.00 13.33 A N ATOM 1515 C HIS A 405 28.760 72.945 8.337 1.00 17.13 A C ATOM 1516 O HIS A 405 29.202 73.961 8.883 1.00 23.80 A O ATOM 1517 N ALA A 406 29.539 72.000 7.815 1.00 16.56 A N ATOM 1518 CA ALA A 406 30.975 71.982 8.042 1.00 14.45 A C ATOM 1519 CB ALA A 406 31.531 70.568 7.875 1.00 19.51 A C ATOM 1520 C ALA A 406 31.665 72.953 7.088 1.00 21.47 A C ATOM 1521 O ALA A 406 32.869 73.170 7.192 1.00 18.14 A O ATOM 1522 N LEU A 407 30.877 73.512 6.167 1.00 16.93 A N ATOM 1523 CA LEU A 407 31.311 74.572 5.267 1.00 18.49 A C ATOM 1524 CB LEU A 407 30.833 74.281 3.837 1.00 16.07 A C ATOM 1525 CG LEU A 407 31.341 72.992 3.177 1.00 19.22 A C ATOM 1526 CD1 LEU A 407 30.919 72.942 1.697 1.00 18.00 A C ATOM 1527 CD2 LEU A 407 32.869 72.878 3.321 1.00 13.08 A C ATOM 1528 C LEU A 407 30.752 75.925 5.710 1.00 17.72 A C ATOM 1529 O LEU A 407 31.103 76.962 5.143 1.00 17.69 A O ATOM 1530 N GLY A 408 29.858 75.903 6.695 1.00 22.14 A N ATOM 1531 CA GLY A 408 29.282 77.121 7.255 1.00 19.75 A C ATOM 1532 C GLY A 408 27.759 77.246 7.200 1.00 20.64 A C ATOM 1533 O GLY A 408 27.196 78.189 7.758 1.00 22.87 A O ATOM 1534 N LEU A 409 27.084 76.313 6.534 1.00 17.60 A N ATOM 1535 CA LEU A 409 25.632 76.446 6.322 1.00 20.50 A C ATOM 1536 CB LEU A 409 25.131 75.556 5.170 1.00 15.17 A C ATOM 1537 CG LEU A 409 25.675 75.867 3.768 1.00 20.40 A C ATOM 1538 CD1 LEU A 409 25.071 74.939 2.679 1.00 17.45 A C ATOM 1539 CD2 LEU A 409 25.410 77.329 3.420 1.00 18.87 A C ATOM 1540 C LEU A 409 24.819 76.139 7.568 1.00 21.48 A C ATOM 1541 O LEU A 409 25.130 75.221 8.311 1.00 19.29 A O ATOM 1542 N ASP A 410 23.757 76.910 7.764 1.00 21.66 A N ATOM 1543 CA ASP A 410 22.773 76.666 8.809 1.00 23.58 A C ATOM 1544 CB ASP A 410 22.197 78.001 9.298 1.00 23.76 A C ATOM 1545 CG ASP A 410 23.159 78.776 10.171 1.00 33.81 A C ATOM 1546 OD1 ASP A 410 24.149 78.190 10.656 1.00 26.62 A O ATOM 1547 OD2 ASP A 410 22.916 79.984 10.382 1.00 38.25 A O ATOM 1548 C ASP A 410 21.610 75.858 8.248 1.00 22.92 A C ATOM 1549 O ASP A 410 21.516 75.639 7.047 1.00 21.45 A O ATOM 1550 N HIS A 411 20.675 75.476 9.106 1.00 23.41 A N ATOM 1551 CA HIS A 411 19.474 74.823 8.599 1.00 17.58 A C ATOM 1552 CB HIS A 411 18.621 74.265 9.730 1.00 20.90 A C ATOM 1553 CG HIS A 411 19.184 73.018 10.327 1.00 19.34 A C ATOM 1554 CD2 HIS A 411 19.806 71.963 9.751 1.00 17.17 A C ATOM 1555 ND1 HIS A 411 19.197 72.783 11.683 1.00 18.38 A N ATOM 1556 CE1 HIS A 411 19.781 71.621 11.921 1.00 17.55 A C ATOM 1557 NE2 HIS A 411 20.155 71.103 10.765 1.00 17.29 A N ATOM 1558 C HIS A 411 18.645 75.734 7.709 1.00 21.00 A C ATOM 1559 O HIS A 411 18.748 76.950 7.774 1.00 24.03 A O ATOM 1560 N SER A 412 17.825 75.111 6.876 1.00 18.89 A N ATOM 1561 CA SER A 412 16.922 75.807 5.980 1.00 23.36 A C ATOM 1562 CB SER A 412 17.091 75.240 4.570 1.00 17.48 A C ATOM 1563 OG SER A 412 16.056 75.677 3.716 1.00 20.87 A O ATOM 1564 C SER A 412 15.497 75.568 6.448 1.00 18.23 A C ATOM 1565 O SER A 412 15.211 74.544 7.061 1.00 16.35 A O ATOM 1566 N SER A 413 14.599 76.492 6.122 1.00 23.17 A N ATOM 1567 CA SER A 413 13.185 76.340 6.450 1.00 18.90 A C ATOM 1568 CB SER A 413 12.604 77.678 6.939 1.00 22.40 A C ATOM 1569 OG SER A 413 12.647 78.641 5.901 1.00 35.17 A O ATOM 1570 C SER A 413 12.385 75.756 5.272 1.00 23.12 A C ATOM 1571 O SER A 413 11.220 75.382 5.415 1.00 26.66 A O ATOM 1572 N VAL A 414 13.033 75.653 4.119 1.00 21.85 A N ATOM 1573 CA VAL A 414 12.472 74.956 2.967 1.00 26.76 A C ATOM 1574 CB VAL A 414 13.204 75.398 1.675 1.00 22.83 A C ATOM 1575 CG1 VAL A 414 12.639 74.718 0.451 1.00 18.19 A C ATOM 1576 CG2 VAL A 414 13.122 76.916 1.538 1.00 24.67 A C ATOM 1577 C VAL A 414 12.565 73.443 3.175 1.00 23.41 A C ATOM 1578 O VAL A 414 13.664 72.893 3.231 1.00 20.83 A O ATOM 1579 N PRO A 415 11.409 72.763 3.296 1.00 20.31 A N ATOM 1580 CD PRO A 415 10.056 73.326 3.175 1.00 24.76 A C ATOM 1581 CA PRO A 415 11.373 71.350 3.706 1.00 21.38 A C ATOM 1582 CB PRO A 415 9.871 71.077 3.936 1.00 22.42 A C ATOM 1583 CG PRO A 415 9.244 72.431 4.080 1.00 21.16 A C ATOM 1584 C PRO A 415 11.952 70.352 2.695 1.00 22.35 A C ATOM 1585 O PRO A 415 12.340 69.250 3.090 1.00 22.46 A O ATOM 1586 N GLU A 416 12.031 70.735 1.423 1.00 25.51 A N ATOM 1587 CA GLU A 416 12.565 69.850 0.393 1.00 21.45 A C ATOM 1588 CB GLU A 416 11.907 70.150 −0.959 1.00 26.61 A C ATOM 1589 CG GLU A 416 10.385 69.967 −0.982 1.00 32.11 A C ATOM 1590 CD GLU A 416 9.613 71.152 −0.379 1.00 32.29 A C ATOM 1591 OE1 GLU A 416 10.112 72.306 −0.406 1.00 31.31 A O ATOM 1592 OE2 GLU A 416 8.488 70.922 0.109 1.00 31.77 A O ATOM 1593 C GLU A 416 14.093 69.964 0.271 1.00 24.20 A C ATOM 1594 O GLU A 416 14.750 69.125 −0.358 1.00 24.70 A O ATOM 1595 N ALA A 417 14.641 70.992 0.901 1.00 16.48 A N ATOM 1596 CA ALA A 417 16.057 71.323 0.826 1.00 19.74 A C ATOM 1597 CB ALA A 417 16.278 72.751 1.340 1.00 16.73 A C ATOM 1598 C ALA A 417 16.929 70.371 1.618 1.00 19.17 A C ATOM 1599 O ALA A 417 16.522 69.870 2.658 1.00 17.34 A O ATOM 1600 N LEU A 418 18.152 70.156 1.135 1.00 22.37 A N ATOM 1601 CA LEU A 418 19.131 69.340 1.852 1.00 19.50 A C ATOM 1602 CB LEU A 418 20.429 69.238 1.038 1.00 14.34 A C ATOM 1603 CG LEU A 418 21.578 68.518 1.750 1.00 18.12 A C ATOM 1604 CD1 LEU A 418 21.310 67.015 1.863 1.00 14.68 A C ATOM 1605 CD2 LEU A 418 22.902 68.776 1.061 1.00 17.98 A C ATOM 1606 C LEU A 418 19.415 69.841 3.289 1.00 18.40 A C ATOM 1607 O LEU A 418 19.559 69.035 4.209 1.00 19.39 A O ATOM 1608 N MET A 419 19.513 71.160 3.482 1.00 15.39 A N ATOM 1609 CA MET A 419 19.840 71.714 4.796 1.00 15.22 A C ATOM 1610 CB MET A 419 20.550 73.080 4.697 1.00 14.77 A C ATOM 1611 CG MET A 419 21.913 73.039 4.023 1.00 12.11 A C ATOM 1612 SD MET A 419 22.888 71.579 4.499 1.00 16.87 A S ATOM 1613 CE MET A 419 23.188 71.955 6.237 1.00 16.41 A C ATOM 1614 C MET A 419 18.604 71.803 5.703 1.00 20.28 A C ATOM 1615 O MET A 419 18.671 72.284 6.831 1.00 17.99 A O ATOM 1616 N TYR A 420 17.469 71.318 5.214 1.00 18.67 A N ATOM 1617 CA TYR A 420 16.341 71.135 6.098 1.00 20.33 A C ATOM 1618 CB TYR A 420 15.129 70.638 5.335 1.00 21.73 A C ATOM 1619 CG TYR A 420 13.834 70.762 6.105 1.00 22.01 A C ATOM 1620 CD1 TYR A 420 13.279 72.007 6.398 1.00 20.60 A C ATOM 1621 CE1 TYR A 420 12.084 72.102 7.096 1.00 22.90 A C ATOM 1622 CD2 TYR A 420 13.163 69.634 6.541 1.00 19.51 A C ATOM 1623 CE2 TYR A 420 11.973 69.722 7.233 1.00 17.63 A C ATOM 1624 CZ TYR A 420 11.433 70.950 7.517 1.00 21.67 A C ATOM 1625 OH TYR A 420 10.230 71.017 8.228 1.00 17.31 A O ATOM 1626 C TYR A 420 16.764 70.133 7.163 1.00 19.53 A C ATOM 1627 O TYR A 420 17.453 69.159 6.875 1.00 17.97 A O ATOM 1628 N PRO A 421 16.371 70.379 8.412 1.00 19.34 A N ATOM 1629 CD PRO A 421 15.598 71.526 8.915 1.00 18.90 A C ATOM 1630 CA PRO A 421 16.927 69.559 9.494 1.00 17.69 A C ATOM 1631 CB PRO A 421 16.589 70.367 10.748 1.00 16.91 A C ATOM 1632 CG PRO A 421 15.395 71.177 10.357 1.00 18.01 A C ATOM 1633 C PRO A 421 16.361 68.126 9.574 1.00 14.43 A C ATOM 1634 O PRO A 421 17.083 67.244 9.999 1.00 16.67 A O ATOM 1635 N MET A 422 15.129 67.881 9.142 1.00 20.28 A N ATOM 1636 CA MET A 422 14.602 66.514 9.184 1.00 21.94 A C ATOM 1637 CB MET A 422 13.083 66.473 9.066 1.00 19.96 A C ATOM 1638 CG MET A 422 12.345 67.350 10.048 1.00 24.76 A C ATOM 1639 SD MET A 422 10.575 67.036 9.965 1.00 26.36 A S ATOM 1640 CE MET A 422 9.943 68.445 10.880 1.00 18.38 A C ATOM 1641 C MET A 422 15.200 65.618 8.102 1.00 19.89 A C ATOM 1642 O MET A 422 15.536 66.072 7.015 1.00 22.68 A O ATOM 1643 N TYR A 423 15.329 64.337 8.423 1.00 19.74 A N ATOM 1644 CA TYR A 423 15.749 63.350 7.453 1.00 21.11 A C ATOM 1645 CB TYR A 423 16.180 62.044 8.140 1.00 21.72 A C ATOM 1646 CG TYR A 423 16.533 60.962 7.136 1.00 21.32 A C ATOM 1647 CD1 TYR A 423 15.599 60.007 6.738 1.00 18.43 A C ATOM 1648 CE1 TYR A 423 15.931 59.027 5.795 1.00 20.32 A C ATOM 1649 CD2 TYR A 423 17.791 60.921 6.556 1.00 22.39 A C ATOM 1650 CE2 TYR A 423 18.124 59.958 5.616 1.00 20.32 A C ATOM 1651 CZ TYR A 423 17.192 59.009 5.240 1.00 20.13 A C ATOM 1652 OH TYR A 423 17.536 58.064 4.290 1.00 19.72 A O ATOM 1653 C TYR A 423 14.565 63.073 6.543 1.00 23.33 A C ATOM 1654 O TYR A 423 13.453 62.853 7.033 1.00 23.69 A O ATOM 1655 N ARG A 424 14.805 63.087 5.231 1.00 22.96 A N ATOM 1656 CA ARG A 424 13.835 62.611 4.248 1.00 23.79 A C ATOM 1657 CB ARG A 424 13.025 63.771 3.664 1.00 26.70 A C ATOM 1658 CG ARG A 424 13.783 64.513 2.566 1.00 33.42 A C ATOM 1659 CD ARG A 424 12.923 65.521 1.823 1.00 37.37 A C ATOM 1660 NE ARG A 424 13.678 66.124 0.735 1.00 33.14 A N ATOM 1661 CZ ARG A 424 13.331 66.047 −0.544 1.00 30.07 A C ATOM 1662 NH1 ARG A 424 12.225 65.404 −0.897 1.00 35.26 A N ATOM 1663 NH2 ARG A 424 14.092 66.613 −1.469 1.00 32.21 A N ATOM 1664 C ARG A 424 14.582 61.906 3.115 1.00 27.22 A C ATOM 1665 O ARG A 424 15.349 62.540 2.377 1.00 29.66 A O ATOM 1666 N PHE A 425 14.388 60.598 2.971 1.00 21.31 A N ATOM 1667 CA PHE A 425 15.125 59.896 1.935 1.00 20.42 A C ATOM 1668 CB PHE A 425 15.053 58.381 2.108 1.00 17.81 A C ATOM 1669 CG PHE A 425 15.552 57.621 0.925 1.00 17.63 A C ATOM 1670 CD1 PHE A 425 16.899 57.348 0.777 1.00 20.28 A C ATOM 1671 CD2 PHE A 425 14.677 57.191 −0.052 1.00 18.22 A C ATOM 1672 CE1 PHE A 425 17.362 56.639 −0.338 1.00 21.79 A C ATOM 1673 CE2 PHE A 425 15.130 56.485 −1.151 1.00 23.43 A C ATOM 1674 CZ PHE A 425 16.476 56.208 −1.288 1.00 21.36 A C ATOM 1675 C PHE A 425 14.587 60.317 0.575 1.00 20.67 A C ATOM 1676 O PHE A 425 13.435 60.731 0.453 1.00 26.14 A O ATOM 1677 N THR A 426 15.438 60.234 −0.433 1.00 22.83 A N ATOM 1678 CA THR A 426 15.074 60.615 −1.790 1.00 23.78 A C ATOM 1679 CB THR A 426 15.106 62.145 −1.959 1.00 27.93 A C ATOM 1680 OG1 THR A 426 14.661 62.488 −3.273 1.00 26.52 A O ATOM 1681 CG2 THR A 426 16.521 62.676 −1.760 1.00 27.57 A C ATOM 1682 C THR A 426 16.073 60.005 −2.746 1.00 22.46 A C ATOM 1683 O THR A 426 17.226 59.791 −2.373 1.00 24.24 A O ATOM 1684 N GLU A 427 15.636 59.714 −3.972 1.00 24.46 A N ATOM 1685 CA GLU A 427 16.543 59.234 −5.004 1.00 25.45 A C ATOM 1686 CB GLU A 427 15.923 58.072 −5.785 1.00 24.88 A C ATOM 1687 CG GLU A 427 16.068 56.718 −5.090 1.00 25.39 A C ATOM 1688 CD GLU A 427 14.999 55.717 −5.484 1.00 41.36 A C ATOM 1689 OE1 GLU A 427 13.957 56.130 −6.046 1.00 46.52 A O ATOM 1690 OE2 GLU A 427 15.195 54.511 −5.220 1.00 44.76 A O ATOM 1691 C GLU A 427 16.906 60.398 −5.924 1.00 25.02 A C ATOM 1692 O GLU A 427 17.839 60.308 −6.709 1.00 22.84 A O ATOM 1693 N GLY A 428 16.174 61.501 −5.806 1.00 27.58 A N ATOM 1694 CA GLY A 428 16.474 62.688 −6.596 1.00 19.87 A C ATOM 1695 C GLY A 428 17.800 63.325 −6.213 1.00 22.23 A C ATOM 1696 O GLY A 428 18.373 63.026 −5.144 1.00 20.97 A O ATOM 1697 N PRO A 429 18.308 64.219 −7.081 1.00 18.13 A N ATOM 1698 CD PRO A 429 17.707 64.651 −8.362 1.00 18.91 A C ATOM 1699 CA PRO A 429 19.518 64.967 −6.756 1.00 17.84 A C ATOM 1700 CB PRO A 429 19.645 65.969 −7.917 1.00 16.81 A C ATOM 1701 CG PRO A 429 18.854 65.325 −9.058 1.00 19.09 A C ATOM 1702 C PRO A 429 19.333 65.700 −5.430 1.00 16.73 A C ATOM 1703 O PRO A 429 18.336 66.402 −5.220 1.00 15.42 A O ATOM 1704 N PRO A 430 20.291 65.527 −4.522 1.00 18.66 A N ATOM 1705 CD PRO A 430 21.387 64.540 −4.588 1.00 16.46 A C ATOM 1706 CA PRO A 430 20.121 66.058 −3.167 1.00 16.69 A C ATOM 1707 CB PRO A 430 21.356 65.520 −2.436 1.00 19.56 A C ATOM 1708 CG PRO A 430 21.615 64.208 −3.109 1.00 13.45 A C ATOM 1709 C PRO A 430 20.029 67.595 −3.057 1.00 18.52 A C ATOM 1710 O PRO A 430 19.242 68.080 −2.247 1.00 14.26 A O ATOM 1711 N LEU A 431 20.780 68.344 −3.859 1.00 12.35 A N ATOM 1712 CA LEU A 431 20.774 69.793 −3.716 1.00 16.93 A C ATOM 1713 CB LEU A 431 22.038 70.414 −4.317 1.00 13.30 A C ATOM 1714 CG LEU A 431 23.347 69.980 −3.668 1.00 18.77 A C ATOM 1715 CD1 LEU A 431 24.550 70.368 −4.530 1.00 12.81 A C ATOM 1716 CD2 LEU A 431 23.462 70.536 −2.254 1.00 16.61 A C ATOM 1717 C LEU A 431 19.548 70.484 −4.305 1.00 17.06 A C ATOM 1718 O LEU A 431 19.010 70.073 −5.331 1.00 15.66 A O ATOM 1719 N HIS A 432 19.124 71.548 −3.638 1.00 17.17 A N ATOM 1720 CA HIS A 432 18.039 72.394 −4.120 1.00 18.04 A C ATOM 1721 CB HIS A 432 16.814 72.264 −3.194 1.00 17.82 A C ATOM 1722 CO HIS A 432 16.084 70.965 −3.360 1.00 16.24 A C ATOM 1723 CD2 HIS A 432 14.880 70.683 −3.909 1.00 17.82 A C ATOM 1724 ND1 HIS A 432 16.628 69.751 −2.987 1.00 19.06 A N ATOM 1725 CE1 HIS A 432 15.780 68.781 −3.286 1.00 17.03 A C ATOM 1726 NE2 HIS A 432 14.712 69.321 −3.847 1.00 20.61 A N ATOM 1727 C HIS A 432 18.531 73.831 −4.207 1.00 16.84 A C ATOM 1728 O HIS A 432 19.624 74.144 −3.737 1.00 15.57 A O ATOM 1729 N LYS A 433 17.729 74.697 −4.816 1.00 15.30 A N ATOM 1730 CA LYS A 433 18.089 76.092 −5.013 1.00 18.53 A C ATOM 1731 CB LYS A 433 16.885 76.848 −5.567 1.00 16.42 A C ATOM 1732 CG LYS A 433 16.437 76.421 −6.965 1.00 16.12 A C ATOM 1733 CD LYS A 433 15.053 76.999 −7.263 1.00 17.15 A C ATOM 1734 CE LYS A 433 14.558 76.604 −8.661 1.00 23.44 A C ATOM 1735 NZ LYS A 433 15.422 77.208 −9.710 1.00 17.67 A N ATOM 1736 C LYS A 433 18.524 76.771 −3.724 1.00 19.85 A C ATOM 1737 O LYS A 433 19.440 77.611 −3.720 1.00 19.71 A O ATOM 1738 N ASP A 434 17.815 76.458 −2.646 1.00 19.72 A N ATOM 1739 CA ASP A 434 18.094 77.050 −1.345 1.00 17.66 A C ATOM 1740 CB ASP A 434 17.073 76.577 −0.325 1.00 17.41 A C ATOM 1741 CG ASP A 434 17.021 77.467 0.873 1.00 20.80 A C ATOM 1742 OD1 ASP A 434 16.602 78.637 0.709 1.00 19.19 A O ATOM 1743 OD2 ASP A 434 17.414 77.005 1.967 1.00 23.04 A O ATOM 1744 C ASP A 434 19.498 76.716 −0.852 1.00 16.49 A C ATOM 1745 O ASP A 434 20.231 77.598 −0.366 1.00 16.36 A O ATOM 1746 N ASP A 435 19.873 75.444 −0.969 1.00 15.24 A N ATOM 1747 CA ASP A 435 21.215 75.011 −0.571 1.00 13.76 A C ATOM 1748 CB ASP A 435 21.361 73.474 −0.635 1.00 13.65 A C ATOM 1749 CG ASP A 435 20.186 72.742 −0.018 1.00 14.94 A C ATOM 1750 OD1 ASP A 435 19.962 72.882 1.207 1.00 16.15 A O ATOM 1751 OD2 ASP A 435 19.484 72.015 −0.758 1.00 20.89 A O ATOM 1752 C ASP A 435 22.295 75.671 −1.445 1.00 16.71 A C ATOM 1753 O ASP A 435 23.352 76.082 −0.945 1.00 21.20 A O ATOM 1754 N VAL A 436 22.052 75.756 −2.747 1.00 20.97 A N ATOM 1755 CA VAL A 436 23.092 76.273 −3.655 1.00 16.69 A C ATOM 1756 CB VAL A 436 22.788 75.979 −5.133 1.00 17.52 A C ATOM 1757 CG1 VAL A 436 23.832 76.659 −6.038 1.00 13.35 A C ATOM 1758 CG2 VAL A 436 22.697 74.436 −5.414 1.00 11.72 A C ATOM 1759 C VAL A 436 23.264 77.787 −3.433 1.00 15.65 A C ATOM 1760 O VAL A 436 24.379 78.310 −3.327 1.00 17.23 A O ATOM 1761 N ASN A 437 22.144 78.483 −3.353 1.00 18.51 A N ATOM 1762 CA ASN A 437 22.162 79.899 −3.057 1.00 17.03 A C ATOM 1763 CB ASN A 437 20.752 80.467 −3.168 1.00 23.11 A C ATOM 1764 CG ASN A 437 20.297 80.595 −4.609 1.00 23.27 A C ATOM 1765 OD1 ASN A 437 21.090 80.420 −5.538 1.00 23.74 A O ATOM 1766 ND2 ASN A 437 19.018 80.883 −4.809 1.00 26.53 A N ATOM 1767 C ASN A 437 22.781 80.167 −1.685 1.00 23.58 A C ATOM 1768 O ASN A 437 23.538 81.123 −1.512 1.00 21.25 A O ATOM 1769 N GLY A 438 22.500 79.284 −0.728 1.00 17.14 A N ATOM 1770 CA GLY A 438 23.045 79.422 0.610 1.00 20.64 A C ATOM 1771 C GLY A 438 24.559 79.422 0.573 1.00 26.22 A C ATOM 1772 O GLY A 438 25.225 80.279 1.170 1.00 27.43 A O ATOM 1773 N ILE A 439 25.117 78.456 −0.139 1.00 20.58 A N ATOM 1774 CA ILE A 439 26.559 78.329 −0.217 1.00 24.44 A C ATOM 1775 CB ILE A 439 26.980 76.891 −0.645 1.00 23.24 A C ATOM 1776 CG2 ILE A 439 26.913 76.722 −2.141 1.00 22.12 A C ATOM 1777 CG1 ILE A 439 28.360 76.538 −0.086 1.00 23.37 A C ATOM 1778 CD1 ILE A 439 28.421 76.519 1.447 1.00 21.30 A C ATOM 1779 C ILE A 439 27.180 79.417 −1.117 1.00 25.93 A C ATOM 1780 O ILE A 439 28.270 79.909 −0.830 1.00 25.28 A O ATOM 1781 N ARG A 440 26.486 79.800 −2.186 1.00 25.31 A N ATOM 1782 CA ARG A 440 26.980 80.874 −3.047 1.00 26.15 A C ATOM 1783 CB ARG A 440 26.077 81.092 −4.262 1.00 25.27 A C ATOM 1784 CG ARG A 440 26.093 79.982 −5.282 1.00 25.92 A C ATOM 1785 CD ARG A 440 25.257 80.362 −6.486 1.00 29.79 A C ATOM 1786 NE ARG A 440 25.934 81.336 −7.350 1.00 24.11 A N ATOM 1787 CZ ARG A 440 25.541 81.611 −8.588 1.00 27.82 A C ATOM 1788 NH1 ARG A 440 24.475 80.993 −9.088 1.00 26.26 A N ATOM 1789 NH2 ARG A 440 26.207 82.491 −9.328 1.00 21.28 A N ATOM 1790 C ARG A 440 27.090 82.178 −2.267 1.00 27.53 A C ATOM 1791 O ARG A 440 28.041 82.946 −2.453 1.00 31.84 A O ATOM 1792 N HIS A 441 26.106 82.424 −1.403 1.00 29.10 A N ATOM 1793 CA HIS A 441 26.079 83.619 −0.569 1.00 28.90 A C ATOM 1794 CB HIS A 441 24.697 83.808 0.068 1.00 30.71 A C ATOM 1795 CG HIS A 441 23.591 84.022 −0.914 1.00 30.92 A C ATOM 1796 CD2 HIS A 441 22.246 84.039 −0.748 1.00 26.53 A C ATOM 1797 ND1 HIS A 441 23.814 84.252 −2.255 1.00 24.41 A N ATOM 1798 CE1 HIS A 441 22.656 84.410 −2.871 1.00 25.22 A C ATOM 1799 NE2 HIS A 441 21.688 84.276 −1.981 1.00 29.06 A N ATOM 1800 C HIS A 441 27.129 83.545 0.540 1.00 30.68 A C ATOM 1801 O HIS A 441 27.157 84.395 1.425 1.00 29.55 A O ATOM 1802 N LEU A 442 27.975 82.520 0.490 1.00 28.39 A N ATOM 1803 CA LEU A 442 28.982 82.289 1.514 1.00 28.94 A C ATOM 1804 CB LEU A 442 28.710 80.953 2.208 1.00 34.10 A C ATOM 1805 CG LEU A 442 29.489 80.668 3.488 1.00 36.13 A C ATOM 1806 CD1 LEU A 442 29.759 81.966 4.233 1.00 32.27 A C ATOM 1807 CD2 LEU A 442 28.721 79.680 4.353 1.00 25.97 A C ATOM 1808 C LEU A 442 30.413 82.301 0.981 1.00 32.13 A C ATOM 1809 O LEU A 442 31.315 82.872 1.598 1.00 32.29 A O ATOM 1810 N TYR A 443 30.629 81.652 −0.157 1.00 30.74 A N ATOM 1811 CA TYR A 443 31.968 81.531 −0.714 1.00 28.94 A C ATOM 1812 CB TYR A 443 32.384 80.051 −0.830 1.00 30.85 A C ATOM 1813 CG TYR A 443 32.712 79.388 0.502 1.00 29.82 A C ATOM 1814 CD1 TYR A 443 31.787 78.569 1.144 1.00 26.51 A C ATOM 1815 CE1 TYR A 443 32.084 77.967 2.360 1.00 23.42 A C ATOM 1816 CD2 TYR A 443 33.949 79.583 1.115 1.00 28.80 A C ATOM 1817 CE2 TYR A 443 34.259 78.981 2.343 1.00 23.90 A C ATOM 1818 CZ TYR A 443 33.316 78.177 2.961 1.00 20.93 A C ATOM 1819 OH TYR A 443 33.598 77.574 4.179 1.00 25.03 A O ATOM 1820 C TYR A 443 32.024 82.214 −2.080 1.00 38.07 A C ATOM 1821 O TYR A 443 31.212 81.921 −2.959 1.00 33.93 A O ATOM 1822 ZN ZN A 500 21.724 69.882 10.344 1.00 19.81 A Zn ATOM 1823 ZN ZN A 501 29.842 64.678 18.223 1.00 27.41 A Zn ATOM 1824 CA CA A 502 20.215 58.596 17.390 1.00 28.51 A Ca ATOM 1825 CA CA A 504 38.342 70.185 12.627 1.00 41.48 A Ca ATOM 1826 CA CA A 505 41.195 78.710 7.741 1.00 45.09 A Ca TER 1827 CA A 505 END

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1. A method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of proMMP9 comprising the steps of: a. employing the structural coordinates of the allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding pocket on a computer, wherein said computer comprises the means for generating said three-dimensional model; b. identifying said allosteric binding site of proMMP9, wherein said allosteric binding site comprises a region of space that is occupied by phenylalanine (Phe) 107 in the apo form of proMMP9, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); c. employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.
 2. The method of claim 1, wherein said allosteric binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).
 3. A method for designing, selecting and/or optimizing a chemical entity that binds to an allosteric binding site of a homologue of proMMP9 comprising the steps of: a. employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of said homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; b. identifying said allosteric binding site of the homologue of proMMP9, wherein said allosteric binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; c. employing the residues identified in (b) to design, select and/or optimize said chemical entity by performing a fitting operation between said chemical entity and said three-dimensional structural information of all or part of said allosteric binding site.
 4. The method of claim 3, wherein said allosteric binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).
 5. A method for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9 comprising the steps of: a. employing the structural coordinates of said allosteric binding site of proMMP9 according to any to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; b. identifying a binding site for said chemical entity, wherein said binding site comprises a region of space that is occupied by Phe 107 in the apo form of proMMP9, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1); c. employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and d. analyzing the results of said fitting operation to quantitate the association between the chemical entity and all or part of the allosteric binding site.
 6. The method of claim 5, wherein said allosteric binding site comprises amino acid residues 100-102, 110, 114, 177-179, 190-193, and 405-410, numbering taken from full-length human matrix metalloproteinase-9 precursor, proMMP9(1-707) (SEQ ID NO:1).
 7. A method for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9 comprising the steps of: a. employing the structural coordinates of proMMP9 according to any to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on a computer, wherein said computer comprises the means for generating said three-dimensional model; b. identifying a binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; c. employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and d. analyzing the results of said fitting operation to quantitate the association between the chemical entity and all or part of the allosteric binding site.
 8. A method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: a. employing the structural coordinates of said allosteric binding site of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of proMMP9 on said computer; b. identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region of space that is occupied by Phe 107 in the apo form of proMMP9; c. employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and d. analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site.
 9. The method according to claim 8, further comprising the steps of: (e) repeating steps (a) through (d) with a second chemical entity; and (f) selecting at least one part of said first or second chemical entity that associates with said all or part of said allosteric binding site based on said quantitated association of said first or second chemical entity.
 10. A method of employing a computer for evaluating the ability of a chemical entity to associate with all or part of an allosteric binding site of a homologue of proMMP9, wherein said computer comprises a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates of the allosteric binding site according to any one of Tables 11-14 and means for generating a three-dimensional graphical representation of the allosteric binding site, and wherein said method comprises the steps of: a. employing the structural coordinates of proMMP9 according to any one of Tables 11-14 to generate a three-dimensional model of said allosteric binding site of the homologue of proMMP9 on said computer; b. identifying an allosteric binding site for said chemical entity, wherein said binding site comprises a region that is homologous to the region of space that is occupied by Phe 107 in the apo form of proMMP9; c. employing computational means to perform a fitting operation between the chemical entity and all or part of the allosteric binding site identified in (b); and d. analyzing the results of said fitting operation to quantitate the association between said chemical entity and all or part of the allosteric binding site.
 11. The method according to claim 10, further comprising the steps of: (e) repeating steps (a) through (d) with a second chemical entity; and (f) selecting at least one part of said first or second chemical entity that associates with said all or part of said allosteric binding site based on said quantitated association of said first or second chemical entity.
 10. The method of claim 8 or 9, wherein said homologue of proMMP9 is selected from the group consisting of: proMMP1, proMMP2, proMMP3, and proMMP13. 